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Conserved domains on  [gi|313569791|ref|NP_000478|]
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arylsulfatase A isoform a precursor [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 10888432)

alkaline phosphatase (ALP) family protein may catalyze the hydrolysis of substrates; the ALP superfamily includes alkaline phosphatases and sulfatases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
22-505 0e+00

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


:

Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 864.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16158    1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPI 181
Cdd:cd16158   81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16158  161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 341
Cdd:cd16158  241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 342 LAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSS 421
Cdd:cd16158  321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 422 LTAHEPPLLYDLSKDPGENYNLLGgvagaTPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPAC 501
Cdd:cd16158  401 LTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSC 475

                 ....
gi 313569791 502 CHCP 505
Cdd:cd16158  476 CQCH 479
 
Name Accession Description Interval E-value
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
22-505 0e+00

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 864.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16158    1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPI 181
Cdd:cd16158   81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16158  161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 341
Cdd:cd16158  241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 342 LAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSS 421
Cdd:cd16158  321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 422 LTAHEPPLLYDLSKDPGENYNLLGgvagaTPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPAC 501
Cdd:cd16158  401 LTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSC 475

                 ....
gi 313569791 502 CHCP 505
Cdd:cd16158  476 CQCH 479
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-454 5.23e-113

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 339.93  E-value: 5.23e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvLVPSSRG 100
Cdd:COG3119   22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD--NGEGYNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipYSHDqgpcqnltcfppatpcdggcdqglvp 180
Cdd:COG3119  100 GLPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD-------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 181 ipllanlsveaqppwlpgleaRYMAFAHDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQSFAE--------- 242
Cdd:COG3119  132 ---------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldKYDGKDIPLppnlaprdl 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 -----RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmsrGGCSGlLRCGKGTTYEGGVREPAL 317
Cdd:COG3119  191 teeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG-LRGGKGTLYEGGIRVPLI 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 318 AFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDEvRGVFAVRTGKY 396
Cdd:COG3119  264 VRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYLYWE--YPRG-GGNRAIRTGRW 339
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 313569791 397 KAHFFTQGSahsdttadpachasssltahEPPLLYDLSKDPGENYNLlggvAGATPEV 454
Cdd:COG3119  340 KLIRYYDDD--------------------GPWELYDLKNDPGETNNL----AADYPEV 373
Sulfatase pfam00884
Sulfatase;
23-348 2.91e-70

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 226.54  E-value: 2.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791   23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvPSSRGGL 102
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflPPHQGFHRFLGIPYSHDQgpcQNLTCFPPATPCDGGCdqglvpip 182
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFGRNTGSDL---YADPPDVPYNCSGGGV-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  183 llanlsveaqppwlpgLEARYMAFAHDLmadAQRQDRPFFLYYASHHTHYP------------QFSGQSFAERSGRGPFG 250
Cdd:pfam00884 143 ----------------SDEALLDEALEF---LDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSEEQLLNSYD 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  251 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmSRGGCSGLLRCGKG-TTYEGGVREPALAFWPGHIAPG-V 328
Cdd:pfam00884 204 NTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGqK 278
                         330       340
                  ....*....|....*....|
gi 313569791  329 THELASSLDLLPTLAALAGA 348
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
PRK13759 PRK13759
arylsulfatase; Provisional
23-445 3.50e-34

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 134.41  E-value: 3.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLgYGD-LGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMypgvlVPSSRGG 101
Cdd:PRK13759   7 PNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR-----VGYGDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLpphqGFHRFL---GIPYS-HDQGPCQN------LTCFPPATPcd 171
Cdd:PRK13759  81 PWNYKNTLPQEFRDAGYYTQCIGKMH--VFPQRNLL----GFHNVLlhdGYLHSgRNEDKSQFdfvsdyLAWLREKAP-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 172 gGCDQGLVPIPLLANlSVEAQpPWlpGLEARY------MAFAHDLMadaQRQDR--PFFLY--YASHHTHY--PQF---- 235
Cdd:PRK13759 153 -GKDPDLTDIGWDCN-SWVAR-PW--DLEERLhptnwvGSESIEFL---RRRDPtkPFFLKmsFARPHSPYdpPKRyfdm 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 236 -----------SGQSFAERSG---------RGPFGDSLME------------LDAAVGTLMTAIGDLGLLEETLVIFTAD 283
Cdd:PRK13759 225 ykdadipdphiGDWEYAEDQDpeggsidalRGNLGEEYARraraayyglithIDHQIGRFLQALKEFGLLDNTIILFVSD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 284 NGpETMrmsrgGCSGLLRcgKGTTYEGGVREPALAFWPGHIAPG----VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 359
Cdd:PRK13759 305 HG-DML-----GDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLAGGTIPD-DVDGRS 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 360 LSPLLLGTGKSPRQSL-----FFYPS--YpdevrgvfaVRTGKYKAHFFTQgsahsdttadpachassslTAHEPplLYD 432
Cdd:PRK13759 376 LKNLIFGQYEGWRPYLhgehaLGYSSdnY---------LTDGKWKYIWFSQ-------------------TGEEQ--LFD 425
                        490
                 ....*....|...
gi 313569791 433 LSKDPGENYNLLG 445
Cdd:PRK13759 426 LKKDPHELHNLSP 438
 
Name Accession Description Interval E-value
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
22-505 0e+00

Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.


Pssm-ID: 293777 [Multi-domain]  Cd Length: 479  Bit Score: 864.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16158    1 PPNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPI 181
Cdd:cd16158   81 LPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGIPYSHDQGPCQNLTCFPPNIPCFGGCDQGEVPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16158  161 PLFYNESIVQQPVDLLTLEERYAKFAKDFIADNAKEGKPFFLYYASHHTHYPQFAGQKFAGRSSRGPFGDALAELDGSVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPT 341
Cdd:cd16158  241 ELLQTLKENGIDNNTLVFFTSDNGPSTMRKSRGGNAGLLKCGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 342 LAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSS 421
Cdd:cd16158  321 IAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTPDKDCHPSAE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 422 LTAHEPPLLYDLSKDPGENYNLLGgvagaTPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPAC 501
Cdd:cd16158  401 LTSHDPPLLFDLSQDPSENYNLLG-----LPEYNQVLKQIQQVKERFEASMKFGESEINKGEDPALEPCCKPGCTPKPSC 475

                 ....
gi 313569791 502 CHCP 505
Cdd:cd16158  476 CQCH 479
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
22-443 0e+00

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293750 [Multi-domain]  Cd Length: 399  Bit Score: 562.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGG 101
Cdd:cd16026    1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVGPPGSKGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPatpcdggcdqgLVPI 181
Cdd:cd16026   81 LPPDEITIAEVLKKAGYRTALVGKWHLGHQPE--FLPTRHGFDEYFGIPYSNDMWPFPLYRNDPP-----------GPLP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 PLLANLSVEAQPPWLPGLEARYMAFAHDLMADAqrQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVG 261
Cdd:cd16026  148 PLMENEEVIEQPADQSSLTQRYTDEAVDFIERN--KDQPFFLYLAHTMPHVPLFASEKFKGRSGAGLYGDVVEELDWSVG 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 262 TLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLP 340
Cdd:cd16026  226 RILDALKELGLEENTLVIFTSDNGPWLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGtVSDELASTMDLLP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 341 TLAALAGAPLPN-VTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDevrgVFAVRTGKYKAHFFTQGSAHSDTtadpachAS 419
Cdd:cd16026  306 TLAALAGAPLPEdRVIDGKDISPLLLGGSKSPPHPFFYYYDGGD----LQAVRSGRWKLHLPTTYRTGTDP-------GG 374
                        410       420
                 ....*....|....*....|....
gi 313569791 420 SSLTAHEPPLLYDLSKDPGENYNL 443
Cdd:cd16026  375 LDPTKLEPPLLYDLEEDPGETYNV 398
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
23-443 3.90e-134

sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous 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: 293779 [Multi-domain]  Cd Length: 445  Bit Score: 395.64  E-value: 3.90e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPG--VLVPSSRG 100
Cdd:cd16160    2 PNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGtrVFLPWDIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHrFLG--IPYSHdqgpcqNLTCFPPATPCDGGc 174
Cdd:cd16160   82 GLPKTEVTMAEALKEAGYTTGMVGKWHLGINENnhsdGAHLPSHHGFD-FVGtnLPFTN------SWACDDTGRHVDFP- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 175 DQGLVPipLLANLSVEAQPPWLPGLEARYMAFAHDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLM 254
Cdd:cd16160  154 DRSACF--LYYNDTIVEQPIQHEHLTETLVGDAKSFIED--NQENPFFLYFSFPQTHTPLFASKRFKGKSKRGRYGDNIN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 255 ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELAS 334
Cdd:cd16160  230 EMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPHVEYCLEGGSTGGLKGGKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVS 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 335 SLDLLPTLAALAGAPLPNVT-LDGFDLSPLLLGTGKSPRQSLFFYpsYPDEvrgVFAVRTGKYKAHFFTQgSAHSDTTAD 413
Cdd:cd16160  310 TMDIFPTFVDLAGGTLPTDRiYDGLSITDLLLGEADSPHDDILYY--CCSR---LMAVRYGSYKIHFKTQ-PLPSQESLD 383
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 313569791 414 PACHA--------------SSSLTAHEPPLLYDLSKDPGENYNL 443
Cdd:cd16160  384 PNCDGggplsdyivcydceDECVTKHNPPLIFDVEKDPGEQYPL 427
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
23-443 9.95e-122

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: 361.47  E-value: 9.95e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSST---TPNLDQLAAGGLRFTDFYVPVSlCTPSRAALLTGRLPVRMGMYPgVLVPSSR 99
Cdd:cd16142    1 PNILVILGDDIGWGDLGCYGGGIGRgapTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGLTT-VGLPGSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 100 GGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcfppatpcdggcdqglv 179
Cdd:cd16142   79 GGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDG--RLPTDHGFDEFYGNLYHT-------------------------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 180 pipllanlsveaqppwlpgLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHY-----PQFSGQSfaerSGRGPFGDSLM 254
Cdd:cd16142  131 -------------------IDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFptlpsPEFEGKS----SGKGKYADSMV 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 255 ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGcSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELA 333
Cdd:cd16142  188 ELDDHVGQILDALDELGIADNTIVIFTTDNGPEQDVWPDGG-YTPFRGEKGTTWEGGVRVPAIVRWPGKIKPGrVSNEIV 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 334 SSLDLLPTLAALAGAPLPN-------VTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDEVRGvfAVRTGKYKAHFFTQgsa 406
Cdd:cd16142  267 SHLDWFPTLAALAGAPDPKdkllgkdRHIDGVDQSPFLLGKSEKSRRSEFFY--FGEGELG--AVRWKNWKVHFKAQ--- 339
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 313569791 407 hsDTTADPACHASSSLTAhepPLLYDLSKDPGENYNL 443
Cdd:cd16142  340 --EDTGGPTGEPFYVLTF---PLIFNLRRDPKERYDV 371
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
22-443 1.02e-119

arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.


Pssm-ID: 293780 [Multi-domain]  Cd Length: 383  Bit Score: 356.78  E-value: 1.02e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSST-TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMyPGVLVPSSRG 100
Cdd:cd16161    1 KPNFLLLFADDLGWGDLGANWAPNAIlTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGV-GHNFLPTSVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVgpEGAFLPPHQGFHRFLGIPYSHDQGpcqnltcfppatpcdggcdqglvp 180
Cdd:cd16161   80 GLPLNETTLAEVLRQAGYATGMIGKWHLGQ--REAYLPNSRGFDYYFGIPFSHDSS------------------------ 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 181 ipllanlsveaqppwlpgLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSF-AERSGRGPFGDSLMELDAA 259
Cdd:cd16161  134 ------------------LADRYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFqSPTSGRGPYGDALQEMDDL 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 260 VGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGL--------LRCGKGTTYEGGVREPALAFWPGHIAPGVTHE 331
Cdd:cd16161  196 VGQIMDAVKHAGLKDNTLTWFTSDNGPWEVKCELAVGPGTgdwqgnlgGSVAKASTWEGGHREPAIVYWPGRIPANSTSA 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 332 -LASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGsahsd 409
Cdd:cd16161  276 aLVSTLDIFPTVVALAGASLPpGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGG----- 350
                        410       420       430
                 ....*....|....*....|....*....|....
gi 313569791 410 ttADPACHASSSLTAHEPPLLYDLSKDPGENYNL 443
Cdd:cd16161  351 --ALACCGSTGPKLYHDPPLLFDLEVDPAESFPL 382
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
21-454 5.23e-113

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 339.93  E-value: 5.23e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvLVPSSRG 100
Cdd:COG3119   22 KRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTD--NGEGYNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipYSHDqgpcqnltcfppatpcdggcdqglvp 180
Cdd:COG3119  100 GLPPDEPTLAELLKEAGYRTALFGKWHL----------------------YLTD-------------------------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 181 ipllanlsveaqppwlpgleaRYMAFAHDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQSFAE--------- 242
Cdd:COG3119  132 ---------------------LLTDKAIDFLERQADKDKPFFLYLAFNAPHAPyqapeeyldKYDGKDIPLppnlaprdl 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 -----RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmsrGGCSGlLRCGKGTTYEGGVREPAL 317
Cdd:COG3119  191 teeelRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPS------LGEHG-LRGGKGTLYEGGIRVPLI 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 318 AFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDEvRGVFAVRTGKY 396
Cdd:COG3119  264 VRWPGKIKAGsVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPLLTGEKAEWRDYLYWE--YPRG-GGNRAIRTGRW 339
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 313569791 397 KAHFFTQGSahsdttadpachasssltahEPPLLYDLSKDPGENYNLlggvAGATPEV 454
Cdd:COG3119  340 KLIRYYDDD--------------------GPWELYDLKNDPGETNNL----AADYPEV 373
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
23-453 7.93e-109

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: 329.89  E-value: 7.93e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY------------ 90
Cdd:cd16144    1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITdvipgrrgppdn 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  91 PGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgPEGAFLPPHQGFHRflGIPYSHDQGPcqnltcfppatpc 170
Cdd:cd16144   81 TKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLG--GEGGYGPEDQGFDV--NIGGTGNGGP------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 171 DGGCDQGLVPIPLLANLSveaQPPWLPglearymafahDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAE-- 242
Cdd:cd16144  144 PSYYFPPGKPNPDLEDGP---EGEYLT-----------DRLTDEaidfieQNKDKPFFLYLSHYAVHTPIQARPELIEky 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 RSGRGPFGD--------SLME-LDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVR 313
Cdd:cd16144  210 EKKKKGLRKgqknpvyaAMIEsLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPTSNAPLRGGKGSLYEGGIR 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 314 EPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTG-KSPRQSLFF-YPSY-PDEVRGV 388
Cdd:cd16144  290 VPLIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLVPLLKGGEaDLPRRALFWhFPHYhGQGGRPA 369
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313569791 389 FAVRTGKYK-AHFFTQGSAHsdttadpachasssltahepplLYDLSKDPGENYNLlggvAGATPE 453
Cdd:cd16144  370 SAIRKGDWKlIEFYEDGRVE----------------------LYNLKNDIGETNNL----AAEMPE 409
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
23-443 4.81e-108

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: 327.24  E-value: 4.81e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGhPSST--TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRG 100
Cdd:cd16143    1 PNIVIILADDLGYGDISCYN-PDSKipTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSPP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLG-----VGPEGAFL---------------PPHQGFHRFLGIPYShdqgpcQN 160
Cdd:cd16143   80 LIEPDRVTLAKMLKQAGYRTAMVGKWHLGldwkkKDGKKAATgtgkdvdyskpikggPLDHGFDYYFGIPAS------EV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 161 LtcfppatpcdggcdqglvpiPLLANLSVEaqppwlpglearymafahdLMADAQRQDRPFFLYYASHHTHYPQFSGQSF 240
Cdd:cd16143  154 L--------------------PTLTDKAVE-------------------FIDQHAKKDKPFFLYFALPAPHTPIVPSPEF 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 241 AERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMR----MSRGG--CSGLLRCGKGTTYEGGVRE 314
Cdd:cd16143  195 QGKSGAGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGPSPYAdykeLEKFGhdPSGPLRGMKADIYEGGHRV 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 315 PALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLGTGKSPRQSLFFYPSypdeVRGVFAVR 392
Cdd:cd16143  275 PFIVRWPGKIPAGsVSDQLVSLTDLFATLAAIVGQKLPdNAAEDSFSFLPALLGPKKQEVRESLVHHS----GNGSFAIR 350
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 313569791 393 TGKYKAhFFTQGSAHSDTtadPACHASSSLTAHEpplLYDLSKDPGENYNL 443
Cdd:cd16143  351 KGDWKL-IDGTGSGGFSY---PRGKEKLGLPPGQ---LYNLSTDPGESNNL 394
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
22-443 4.34e-103

galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.


Pssm-ID: 293776 [Multi-domain]  Cd Length: 466  Bit Score: 317.10  E-value: 4.34e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY----------- 90
Cdd:cd16157    1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYttnaharnayt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  91 PGVLVpssrGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaFLPPHQGFHRFLGIPYSHdqgpcqnltcFPPATpc 170
Cdd:cd16157   81 PQNIV----GGIPDSEILLPELLKKAGYRNKIVGKWHLGHRPQ--YHPLKHGFDEWFGAPNCH----------FGPYD-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 171 dggcDQGLVPIPLLANLSVEAQ---------PPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFA 241
Cdd:cd16157  143 ----NKAYPNIPVYRDWEMIGRyyeefkidkKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPFL 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 242 ERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETM-RMSRGGCSGLLRCGKGTTYEGGVREPALAFW 320
Cdd:cd16157  219 GTSQRGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALIsAPEQGGSNGPFLCGKQTTFEGGMREPAIAWW 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 321 PGHIAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLgTGKSPRQSLFFYpsypdevRG--VFAVRTGKY 396
Cdd:cd16157  299 PGHIKPGqVSHQLGSLMDLFTTSLALAGLPIPsDRAIDGIDLLPVLL-NGKEKDRPIFYY-------RGdeLMAVRLGQY 370
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313569791 397 KAHFFT-QGSAHSDTTADPACHAS--SSLTAH------EPPLLYDLSKDPGENYNL 443
Cdd:cd16157  371 KAHFWTwSNSWEEFRKGINFCPGQnvPGVTTHnqtdhtKLPLLFHLGRDPGEKYPI 426
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
22-439 3.56e-101

Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of the active estrogen in tumor cells. ES catalyzes the hydrolysis of E1 sulfate, which is a component of the three-enzyme system that has been implicated in intracrine biosynthesis of estradiol. It is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES consisting of two antiparallel alpha helices that protrude from the roughly spherical molecule. These highly hydrophobic helices anchor the functional domain on the membrane surface facing the ER lumen.


Pssm-ID: 293778 [Multi-domain]  Cd Length: 521  Bit Score: 313.84  E-value: 3.56e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGM-----YPGVLVP 96
Cdd:cd16159    1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMasshgMRVILFT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  97 SSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE----GAFLPPHQGFHRFLGIPYSH------DQGPCQNLTCFPP 166
Cdd:cd16159   81 ASSGGLPPNETTFAEVLKQQGYSTALIGKWHLGLHCEsrndFCHHPLNHGFDYFYGLPLTNlkdcgdGSNGEYDLSFDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 167 ATPCDGGCD--------------------------QGLVPIP--------------LLANLSVEAQPPWLPGLEARYMAF 206
Cdd:cd16159  161 FPLLTAFVLitaltiflllylgavskrffvfllilSLLFISLfflllitnryfnciLMRNHEVVEQPMSLENLTQRLTKE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 207 AHDLMADaqRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 286
Cdd:cd16159  241 AISFLER--NKERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 287 ETMRMSR-----GGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPN-VTLDGFD 359
Cdd:cd16159  319 HLEEISVggeygGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGsVIDEPTSLMDIFPTVAALAGAPLPSdRIIDGRD 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 360 LSPLLLGTGK-SPRQSLFFYPSypDEVRGV-FAVRTGK--YKAHFFTQGSaHSDTTADPA---CHAS-SSLTAHEPPLLY 431
Cdd:cd16159  399 LMPLLTGQEKrSPHEFLFHYCG--AELHAVrYRPRDGGavWKAHYFTPNF-YPGTEGCCGtllCRCFgDSVTHHDPPLLF 475

                 ....*...
gi 313569791 432 DLSKDPGE 439
Cdd:cd16159  476 DLSADPSE 483
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
23-454 2.19e-91

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: 284.83  E-value: 2.19e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMGmypgvlVPSSRGG 101
Cdd:cd16146    1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNFHVsPV--CAPTRAALLTGRYPFRTG------VWHTILG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 ---LPLEEVTVAEVLAARGYLTGMAGKWHLGVGPegAFLPPHQGFHRFLGIpyshdqgpcqnltcfppatpCDGGCDQgl 178
Cdd:cd16146   73 rerMRLDETTLAEVFKDAGYRTGIFGKWHLGDNY--PYRPQDRGFDEVLGH--------------------GGGGIGQ-- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 179 vpIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADA------QRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDS 252
Cdd:cd16146  129 --YPDYWGNDYFDDTYYHNGKFVKTEGYCTDVFFDEaidfieENKDKPFFAYLATNAPHGPLQVPDKYLDPYKDMGLDDK 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 253 L-----M--ELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSR--GGcsglLRCGKGTTYEGGVREPALAFWPGH 323
Cdd:cd16146  207 LaafygMieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGVPKRfnAG----MRGKKGSVYEGGHRVPFFIRWPGK 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 324 IAPG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFY---PSYPDEVRGVFAVRTGKYK 397
Cdd:cd16146  283 ILAGkDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPLLKGeSDPWPERTLFTHsgrWPPPPKKKRNAAVRTGRWR 362
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 313569791 398 ahfFTQGSAhsdttadpachasssltahEPPLLYDLSKDPGENYNllggVAGATPEV 454
Cdd:cd16146  363 ---LVSPKG-------------------FQPELYDIENDPGEEND----VADEHPEV 393
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
23-443 1.59e-90

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


Pssm-ID: 293764 [Multi-domain]  Cd Length: 415  Bit Score: 282.95  E-value: 1.59e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTG----RLPVRMGmypgvlvPSS 98
Cdd:cd16145    1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGlhtgHTRVRGN-------SEP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  99 RGGLPL--EEVTVAEVLAARGYLTGMAGKWHLG-VGPEGAflPPHQGFHRFLGIpysHDQGPCQNLtcFPPATPCDGgcd 175
Cdd:cd16145   74 GGQDPLppDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGH--PTKQGFDYFYGY---LDQVHAHNY--YPEYLWRNG--- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 176 qGLVPIPlLANLSVEAQPPWLPGLEARYmafAHDLMADA------QRQDRPFFLYYAS---H-HTHYPQFSG--QSFAER 243
Cdd:cd16145  144 -EKVPLP-NNVIPPLDEGNNAGGGGGTY---SHDLFTDEaldfirENKDKPFFLYLAYtlpHaPLQVPDDGPykYKPKDP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 244 SGRGPFGDSLME---------LDAAVGTLMTAIGDLGLLEETLVIFTADNGPEtmrmSRGGC---------SGLLRCGKG 305
Cdd:cd16145  219 GIYAYLPWPQPEkayaamvtrLDRDVGRILALLKELGIDENTLVVFTSDNGPH----SEGGSehdpdffdsNGPLRGYKR 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 306 TTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSYpdE 384
Cdd:cd16145  295 SLYEGGIRVPFIARWPGKIPAGsVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQQQHDYLYWEFY--E 371
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313569791 385 VRGVFAVRTGKYKAHFFTQGSahsdttadpachasssltahEPPLLYDLSKDPGENYNL 443
Cdd:cd16145  372 GGGAQAVRMGGWKAVRHGKKD--------------------GPFELYDLSTDPGETNNL 410
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
23-443 2.90e-81

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: 258.25  E-value: 2.90e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGL 102
Cdd:cd16029    1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQHGVILAGEPYGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgAFLPPHQGFHRFLGiPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPip 182
Cdd:cd16029   80 PLNETLLPQYLKELGYATHLVGKWHLGFYTW-EYTPTNRGFDSFYG-YYGGAEDYYTHTSGGANDYGNDDLRDNEEPA-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llanlsveaqppwlPGLEARYMAfahDLMAD-AQR------QDRPFFLYYASHHTHYP-QFSGQSFAERSGRGPFGDS-- 252
Cdd:cd16029  156 --------------WDYNGTYST---DLFTDrAVDiienhdPSKPLFLYLAFQAVHAPlQVPPEYADPYEDKFAHIKDed 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 253 -------LMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSrGGCSGLLRCGKGTTYEGGVREPALaFWPGHI- 324
Cdd:cd16029  219 rrtyaamVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGD-GGSNYPLRGGKNTLWEGGVRVPAF-VWSPLLp 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 325 --APGVTHELASSLDLLPTLAALAGA-PLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFF 401
Cdd:cd16029  297 pkRGTVSDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQWDALSGGAPSPRTEILLNIDDITRTTGGAAIRVGDWKLIVG 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 313569791 402 TQgsahsdttadpachasssltahepplLYDLSKDPGENYNL 443
Cdd:cd16029  377 KP--------------------------LFNIENDPCERNDL 392
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
23-359 2.09e-77

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: 242.73  E-value: 2.09e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvLVPSSRGGL 102
Cdd:cd16022    1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVR---GNVGNGGGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16022   78 PPDEPTLAELLKEAGYRTALIGKWH------------------------------------------------------- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llaNLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPqfsgqsFAersgrgpFGDSLMELDAAVGT 262
Cdd:cd16022  103 ---DEAID----FI----------------ERRDKDKPFFLYVSFNAPHPP------FA-------YYAMVSAIDDQIGR 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 263 LMTAIGDLGLLEETLVIFTADNGPetMRMSRGgcsglLRCGKGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPT 341
Cdd:cd16022  147 ILDALEELGLLDNTLIVFTSDHGD--MLGDHG-----LRGKKGSLYEGGIRVPFIVRWPGKIPAGqVSDALVSLLDLLPT 219
                        330
                 ....*....|....*...
gi 313569791 342 LAALAGAPLPNvTLDGFD 359
Cdd:cd16022  220 LLDLAGIEPPE-GLDGRS 236
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
23-443 2.45e-76

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: 244.73  E-value: 2.45e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvlVPSSRGGL 102
Cdd:cd16027    1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHG---LRSRGFPL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLPPHQGFHRFLGIPYSHDQgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16027   77 PDGVKTLPELLREAGYYTGLIGKTH--YNPDAVFPFDDEMRGPDDGGRNAWDY--------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llanlsVEAQPPWLpglearymafahdlmaDAQRQDRPFFLYYASHHTHYPQFSGQSFAE-------------------R 243
Cdd:cd16027  128 ------ASNAADFL----------------NRAKKGQPFFLWFGFHDPHRPYPPGDGEEPgydpekvkvppylpdtpevR 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 244 SGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetMRMSRggcsgllrcGKGTTYEGGVREPALAFWPGH 323
Cdd:cd16027  186 EDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHG---MPFPR---------AKGTLYDSGLRVPLIVRWPGK 253
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 324 IAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFY----PSYPDEVRgvfAVRTGKYK- 397
Cdd:cd16027  254 IKPGsVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGEKDPGRDYVFAErdrhDETYDPIR---SVRTGRYKy 329
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 313569791 398 AHFFtqgsahsdttadpachasssltahEPPLLYDLSKDPGENYNL 443
Cdd:cd16027  330 IRNY------------------------MPEELYDLKNDPDELNNL 351
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-415 3.49e-76

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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 244.43  E-value: 3.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPvSLCTPSRAALLTGRLPVRMGMYPGVLVPSsrggl 102
Cdd:cd16151    1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPK----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 pleEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCqnltcFPPATPcdggcdqglvpIP 182
Cdd:cd16151   75 ---QKTFGHLLKDAGYATAIAGKWQLGGGRGDGDYPHEFGFDEYCLWQLTETGEKY-----SRPATP-----------TF 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 LLANLSVeaqppwlpgLEARYMAFAHDLMAD------AQRQDRPFFLYYASHHTHYP----------QFSGQSFAERSGR 246
Cdd:cd16151  136 NIRNGKL---------LETTEGDYGPDLFADflidfiERNKDQPFFAYYPMVLVHDPfvptpdspdwDPDDKRKKDDPEY 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 247 gpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNG--PETMRMSRGgcsGLLRCGKGTTYEGGVREPALAFWPGHI 324
Cdd:cd16151  207 --FPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGthRPITSRTNG---REVRGGKGKTTDAGTHVPLIVNWPGLI 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 325 APG-VTHELASSLDLLPTLAALAGAPLP-NVTLDGFDLSPLLLG-TGKSPRQSLFFYPSYPDEVRGVFAVRTGKYK---- 397
Cdd:cd16151  282 PAGgVSDDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFAPQLLGkTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKlyad 361
                        410
                 ....*....|....*...
gi 313569791 398 AHFFtqgsahsDTTADPA 415
Cdd:cd16151  362 GRFF-------DLREDPL 372
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
22-443 1.29e-71

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: 233.10  E-value: 1.29e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSStTPNLDQLAAGGLRFTDFYVpVSLCTPSRAALLTGRLP--VRMGMYPGVL--VPS 97
Cdd:cd16025    2 RPNILLILADDLGFSDLGCFGGEIP-TPNLDALAAEGLRFTNFHT-TALCSPTRAALLTGRNHhqVGMGTMAELAtgKPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  98 SRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflppHQGFHrflgipYSHDqgpcqnLTcfppatpcdggcDQG 177
Cdd:cd16025   80 YEGYLPDSAATIAEVLKDAGYHTYMSGKWHLG----------PDDYY------STDD------LT------------DKA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 178 LvpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFLYYASHHTHYP---------QFSGQ---------- 238
Cdd:cd16025  126 I------------------------------EYIDEQKAPDKPFFLYLAFGAPHAPlqapkewidKYKGKydagwdalre 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 239 ----------------SFAERSGRGPFGDSL-----------ME--------LDAAVGTLMTAIGDLGLLEETLVIFTAD 283
Cdd:cd16025  176 erlerqkelglipadtKLTPRPPGVPAWDSLspeekklearrMEvyaamvehMDQQIGRLIDYLKELGELDNTLIIFLSD 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 284 NGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAP--GVTHELASSLDLLPTLAALAGAPLPNV-------T 354
Cdd:cd16025  256 NGASAEPGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKAkgGIRHQFAHVIDIAPTILELAGVEYPKTvngvpqlP 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 355 LDGFDLSPLLLG-TGKSPRQSLFFypsypdEVRGVFAVRTGKYKAhfftqgsahsdttadpachasssLTAHEPPL---- 429
Cdd:cd16025  336 LDGVSLLPTLDGaAAPSRRRTQYF------ELFGNRAIRKGGWKA-----------------------VALHPPPGwgdq 386
                        490
                 ....*....|....*.
gi 313569791 430 --LYDLSKDPGENYNL 443
Cdd:cd16025  387 weLYDLAKDPSETHDL 402
Sulfatase pfam00884
Sulfatase;
23-348 2.91e-70

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 226.54  E-value: 2.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791   23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvPSSRGGL 102
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSY-----VSTPVGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflPPHQGFHRFLGIPYSHDQgpcQNLTCFPPATPCDGGCdqglvpip 182
Cdd:pfam00884  76 PRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQS--PCNLGFDKFFGRNTGSDL---YADPPDVPYNCSGGGV-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  183 llanlsveaqppwlpgLEARYMAFAHDLmadAQRQDRPFFLYYASHHTHYP------------QFSGQSFAERSGRGPFG 250
Cdd:pfam00884 143 ----------------SDEALLDEALEF---LDNNDKPFFLVLHTLGSHGPpyypdrypekyaTFKPSSCSEEQLLNSYD 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  251 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmSRGGCSGLLRCGKG-TTYEGGVREPALAFWPGHIAPG-V 328
Cdd:pfam00884 204 NTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGE-----SLGEGGGYLHGGKYdNAPEGGYRVPLLIWSPGGKAKGqK 278
                         330       340
                  ....*....|....*....|
gi 313569791  329 THELASSLDLLPTLAALAGA 348
Cdd:pfam00884 279 SEALVSHVDLFPTILDLAGI 298
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
21-445 1.07e-65

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: 218.55  E-value: 1.07e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTgrlpvrmGMYP---GVlVPS 97
Cdd:cd16031    1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILT-------GQYShrhGV-TDN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  98 SRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEgaflPPHQGFHRFLGIPYSHDQGPCQNLTcfppatpcdggcDQG 177
Cdd:cd16031   73 NGPLFDASQPTYPKLLRKAGYQTAFIGKWHLGSGGD----LPPPGFDYWVSFPGQGSYYDPEFIE------------NGK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 178 LVPIP-----LLANLSVEaqppWLpglearymafahdlmaDAQRQDRPFFLYY---ASH--------HTH--------YP 233
Cdd:cd16031  137 RVGQKgyvtdIITDKALD----FL----------------KERDKDKPFCLSLsfkAPHrpftpaprHRGlyedvtipEP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 234 Q------FSGQS-FAERSGRGPFGD--------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGp 286
Cdd:cd16031  197 EtfddddYAGRPeWAREQRNRIRGVldgrfdtpekyqrymkdylrTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 287 etmrmsrggcsglLRCG------KGTTYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 359
Cdd:cd16031  276 -------------FFLGehglfdKRLMYEESIRVPLIIRDPRLIKAGtVVDALVLNIDFAPTILDLAGVPIPE-DMQGRS 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 360 LSPLLLGTGKSPRQSLFFY-----PSYPDeVRGVFAVRTGKYK-AHFFTQGsahsdttadpachassslTAHEpplLYDL 433
Cdd:cd16031  342 LLPLLEGEKPVDWRKEFYYeyyeePNFHN-VPTHEGVRTERYKyIYYYGVW------------------DEEE---LYDL 399
                        490
                 ....*....|..
gi 313569791 434 SKDPGENYNLLG 445
Cdd:cd16031  400 KKDPLELNNLAN 411
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-443 8.54e-59

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: 199.72  E-value: 8.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVpssrggL 102
Cdd:cd16034    2 PNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDVP------L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHLGVGPEG-----AFLPPH---QGF---------HRFLGIPYSHDQGPcqnltcfp 165
Cdd:cd16034   76 PPDAPTIADVLKDAGYRTGYIGKWHLDGPERNdgradDYTPPPerrHGFdywkgyecnHDHNNPHYYDDDGK-------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 166 paTPCDGGcdqglvpipllanlsveaqppWLPGLEARyMAFahDLMADAQRQDRPFFLY--YASHHTHY---PQ-----F 235
Cdd:cd16034  148 --RIYIKG---------------------YSPDAETD-LAI--EYLENQADKDKPFALVlsWNPPHDPYttaPEeyldmY 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 236 SGQSFAERsGRGPFGDSLME---------------LDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 300
Cdd:cd16034  202 DPKKLLLR-PNVPEDKKEEAglredlrgyyamitaLDDNIGRLLDALKELGLLENTIVVFTSDHG-DML-----GSHGLM 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 301 RcgKGTTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYP 379
Cdd:cd16034  275 N--KQVPYEESIRVPFIIRYPGKIkAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDLSPLLLGGKDDEPDSVLLQC 351
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 380 SYP------DEVRGVFAVRTGKYKAhfftqgsahsdttadpachassSLTAHEPPLLYDLSKDPGENYNL 443
Cdd:cd16034  352 FVPfgggsaRDGGEWRGVRTDRYTY----------------------VRDKNGPWLLFDNEKDPYQLNNL 399
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-445 1.33e-49

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: 175.49  E-value: 1.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSS-RGG 101
Cdd:cd16033    1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAySRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcqnltcfPPATPCDGGCDqGLVPi 181
Cdd:cd16033   81 LPPGVETFSEDLREAGYRNGYVGKWHVG-----------------------------------PEETPLDYGFD-EYLP- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 pllanlsVEAQPpwlpglEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQ---------------SFAE---- 242
Cdd:cd16033  124 -------VETTI------EYFLADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEpyldmydpediplpeSFADdfed 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 -----RSGRGPFGDSLME-----------------LDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLL 300
Cdd:cd16033  191 kpyiyRRERKRWGVDTEDeedwkeiiahywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHG-DAL-----GAHRLW 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 301 RcgKGT-TYEGGVREPALAFWPGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLG-TGKSPRQSLFF 377
Cdd:cd16033  265 D--KGPfMYEETYRIPLIIKWPGVIAAGqVVDEFVSLLDLAPTILDLAGVDVPPKV-DGRSLLPLLRGeQPEDWRDEVVT 341
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313569791 378 ---YPSYPDEVRgvfAVRTGKYKAHFftqgsahSDTTADpachasssltahEpplLYDLSKDPGENYNLLG 445
Cdd:cd16033  342 eynGHEFYLPQR---MVRTDRYKYVF-------NGFDID------------E---LYDLESDPYELNNLID 387
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-362 4.81e-47

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: 163.95  E-value: 4.81e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY---PGVLVPSSR 99
Cdd:cd16149    1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHdwiVEGSHGKTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 100 GGLPL--EEVTVAEVLAARGYLTGMAGKWHLGvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcDQG 177
Cdd:cd16149   81 KPEGYleGQTTLPEVLQDAGYRCGLSGKWHLG---------------------------------------------DDA 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 178 LvpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFL---YYASHHTHypqfsgQSFAERSGrgpfgdslm 254
Cdd:cd16149  116 A------------------------------DFLRRRAEAEKPFFLsvnYTAPHSPW------GYFAAVTG--------- 150
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 255 eLDAAVGTLMTAIGDLGLLEETLVIFTADNGpetMRMsrgGCSGLLRCGKGTT----YEGGVREPALAFWPGHIAPG-VT 329
Cdd:cd16149  151 -VDRNVGRLLDELEELGLTENTLVIFTSDNG---FNM---GHHGIWGKGNGTFplnmYDNSVKVPFIIRWPGVVPAGrVV 223
                        330       340       350
                 ....*....|....*....|....*....|....
gi 313569791 330 HELASSLDLLPTLAALAGAPLP-NVTLDGFDLSP 362
Cdd:cd16149  224 DSLVSAYDFFPTLLELAGVDPPaDPRLPGRSFAD 257
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-443 2.14e-46

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: 165.82  E-value: 2.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVS----LCTPSRAALLTGR----LPVRMGMypgvl 94
Cdd:cd16155    3 PNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNAYNMGGwsgaVCVPSRAMLMTGRtlfhAPEGGKA----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  95 vpssrgGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPE------------------GAFLPPH------QGFHrflgip 150
Cdd:cd16155   78 ------AIPSDDKTWPETFKKAGYRTFATGKWHNGFADAaiefleeykdgdkpffmyVAFTAPHdprqapPEYL------ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 151 yshDQGPCQNLTC---FPPATPCDGGcdQGLVPIPLLAnlsveaqpPWlPGLEArymafahdlMADAQRQDrpfflYYA- 226
Cdd:cd16155  146 ---DMYPPETIPLpenFLPQHPFDNG--EGTVRDEQLA--------PF-PRTPE---------AVRQHLAE-----YYAm 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 227 -SHhthypqfsgqsfaersgrgpfgdslmeLDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRGGcSGLLrcGKG 305
Cdd:cd16155  198 iTH---------------------------LDAQIGRILDALEASGELDNTIIVFTSDHG-----LAVGS-HGLM--GKQ 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 306 TTYEGGVREPALAFWPGhIAPG-VTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYpsYPDE 384
Cdd:cd16155  243 NLYEHSMRVPLIISGPG-IPKGkRRDALVYLQDVFPTLCELAGIEIPE-SVEGKSLLPVIRGEKKAVRDTLYGA--YRDG 318
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 313569791 385 VRgvfAVRTGKYKAHFFTQGSAHSdttadpachasssltaheppLLYDLSKDPGENYNL 443
Cdd:cd16155  319 QR---AIRDDRWKLIIYVPGVKRT--------------------QLFDLKKDPDELNNL 354
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-438 4.50e-46

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: 163.48  E-value: 4.50e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGGL 102
Cdd:cd16037    1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVW------DNADPY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHLgVGPEgaflPPHqGFHrflgipysHDQgpcqNLTcfppatpcDGGCDqglvpip 182
Cdd:cd16037   75 DGDVPSWGHALRAAGYETVLIGKLHF-RGED----QRH-GFR--------YDR----DVT--------EAAVD------- 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llanlsveaqppWLpglearymafahdlmADAQRQDRPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdsLME-LD 257
Cdd:cd16037  122 ------------WL---------------REEAADDKPWFLFVGFVAPHFPLIAPQEFydlyVRRARAAYYG--LVEfLD 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 337
Cdd:cd16037  173 ENIGRVLDALEELGLLDNTLIIYTSDHG-DML-----GERGLW--GKSTMYEESVRVPMIISGPGIPAGKRVKTPVSLVD 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 338 LLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVrGVFAVRTGKYKAHFFtqgsahsdttadpach 417
Cdd:cd16037  245 LAPTILEAAGAPPPP-DLDGRSLLPLAEGPDDPDRVVFSEYHAHGSPS-GAFMLRKGRWKYIYY---------------- 306
                        410       420
                 ....*....|....*....|.
gi 313569791 418 asssltAHEPPLLYDLSKDPG 438
Cdd:cd16037  307 ------VGYPPQLFDLENDPE 321
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
23-437 2.54e-43

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: 156.20  E-value: 2.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVlvpssrGGL 102
Cdd:cd16032    1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNA------AEF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PLEEVTVAEVLAARGYLTGMAGKWHLgVGPEgaflpPHQGFhrflgipySHDQgpcqnltcfppatpcdggcdqglvpip 182
Cdd:cd16032   75 PADIPTFAHYLRAAGYRTALSGKMHF-VGPD-----QLHGF--------DYDE--------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llanlsveaqppwlpglEARYMA--FAHDLmadAQRQD-RPFFLYYASHHTHYPQFSGQSF----AERSGRGPFGdSLME 255
Cdd:cd16032  114 -----------------EVAFKAvqKLYDL---ARGEDgRPFFLTVSFTHPHDPYVIPQEYwdlyVRRARRAYYG-MVSY 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 256 LDAAVGTLMTAIGDLGLLEETLVIFTADNGpeTMRMSRGgcsgllRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASS 335
Cdd:cd16032  173 VDDKVGQLLDTLERTGLADDTIVIFTSDHG--DMLGERG------LWYKMSFFEGSARVPLIISAPGRFAPRRVAEPVSL 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 336 LDLLPTLAALAGAPLPNV--TLDGFDLSPLLLGTGKSPRQSlfFYPSYPDEvrGVFA----VRTGKYKahfFTqgsahsd 409
Cdd:cd16032  245 VDLLPTLVDLAGGGTAPHvpPLDGRSLLPLLEGGDSGGEDE--VISEYLAE--GAVApcvmIRRGRWK---FI------- 310
                        410       420
                 ....*....|....*....|....*...
gi 313569791 410 ttadpACHAsssltahEPPLLYDLSKDP 437
Cdd:cd16032  311 -----YCPG-------DPDQLFDLEADP 326
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
22-445 2.50e-42

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: 154.69  E-value: 2.50e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSRGG 101
Cdd:cd16152    1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCF------RNGIP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHLgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqglvpi 181
Cdd:cd16152   75 LPADEKTLAHYFRDAGYETGYVGKWHL----------------------------------------------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 pllanlsveaqppwlpgleARYMA-----FAHDLMADAQrQDRPFFL---YYASHHT----HY--PQFSGQSFAERS--- 244
Cdd:cd16152  102 -------------------AGYRVdaltdFAIDYLDNRQ-KDKPFFLflsYLEPHHQndrdRYvaPEGSAERFANFWvpp 161
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 245 ---GRGpfGDSLMEL----------DAAVGTLMTAIGDLGLLEETLVIFTADNgpetmrmsrgGCSGLLRCG--KGTTYE 309
Cdd:cd16152  162 dlaALP--GDWAEELpdylgccerlDENVGRIRDALKELGLYDNTIIVFTSDH----------GCHFRTRNAeyKRSCHE 229
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 310 GGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSypdEVRGVF 389
Cdd:cd16152  230 SSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPE-EMQGRSLLPLVDGKVEDWRNEVFIQIS---ESQVGR 305
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313569791 390 AVRTGKYKahfftqgSAHSDTTADPACHASSSltAHEPPLLYDLSKDPGENYNLLG 445
Cdd:cd16152  306 AIRTDRWK-------YSVAAPDKDGWKDSGSD--VYVEDYLYDLEADPYELVNLIG 352
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-362 2.42e-39

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: 143.84  E-value: 2.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPssrggl 102
Cdd:cd16148    1 MNVILIVIDSLRADHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWGGPLEP------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 plEEVTVAEVLAARGYLTGMAGkWHLGVGPEGAFlppHQGFHRFLGIPYSHDQGPcqnltcFPPATPCDGGCDQGLvpip 182
Cdd:cd16148   75 --DDPTLAEILRKAGYYTAAVS-SNPHLFGGPGF---DRGFDTFEDFRGQEGDPG------EEGDERAERVTDRAL---- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 183 llanlsveaqpPWLpglearymafahdlmaDAQRQDRPFFL---YYASHHthypqfsgqsfaersgrgPFG--DSLMELD 257
Cdd:cd16148  139 -----------EWL----------------DRNADDDPFFLflhYFDPHE------------------PYLydAEVRYVD 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLD 337
Cdd:cd16148  174 EQIGRLLDKLKELGLLEDTLVIVTSDHG-EEF-----GEHGLYWGHGSNLYDEQLHVPLIIRWPGKEPGKRVDALVSHID 247
                        330       340
                 ....*....|....*....|....*
gi 313569791 338 LLPTLAALAGAPlPNVTLDGFDLSP 362
Cdd:cd16148  248 IAPTLLDLLGVE-PPDYSDGRSLLP 271
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
22-443 8.77e-37

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: 140.79  E-value: 8.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYgDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPgvLVPSSRGG 101
Cdd:cd16030    2 KPNVLFIAVDDLRP-WLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYD--NNSYFRKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPlEEVTVAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPCQNLTCFPPATPcdgGCDQGLVPI 181
Cdd:cd16030   79 AP-DAVTLPQYFKENGYTTAGVGKIF------------HPGIPDGDDDPASWDEPPNPPGPEKYPPGK---LCPGKKGGK 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 182 PLLANLSVEAqppwLPGLEARYM-----AFAHDLMADAQRQDRPFFL--------------------Y------------ 224
Cdd:cd16030  143 GGGGGPAWEA----ADVPDEAYPdgkvaDEAIEQLRKLKDSDKPFFLavgfykphlpfvapkkyfdlYplesiplpnpfd 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 225 ------YASHHTHYPQFSGQSFAERSGR--GPFGDSL-MEL-----------DAAVGTLMTAIGDLGLLEETLVIFTADN 284
Cdd:cd16030  219 pidlpeVAWNDLDDLPKYGDIPALNPGDpkGPLPDEQaRELrqayyasvsyvDAQVGRVLDALEELGLADNTIVVLWSDH 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 285 GpetmrMSRG--GcsgllRCGKGTTYEGGVREPaLAFW-PGHIAPG-VTHELASSLDLLPTLAALAGAPLPNVtLDGFDL 360
Cdd:cd16030  299 G-----WHLGehG-----HWGKHTLFEEATRVP-LIIRaPGVTKPGkVTDALVELVDIYPTLAELAGLPAPPC-LEGKSL 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 361 SPLLLGTGKSPRQslFFYPSYPDEVRGVFAVRTGKYKahfFTQgsaHSDttadpachaSSSLTAHEpplLYDLSKDPGEN 440
Cdd:cd16030  367 VPLLKNPSAKWKD--AAFSQYPRPSIMGYSIRTERYR---YTE---WVD---------FDKVGAEE---LYDHKNDPNEW 426

                 ...
gi 313569791 441 YNL 443
Cdd:cd16030  427 KNL 429
PRK13759 PRK13759
arylsulfatase; Provisional
23-445 3.50e-34

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 134.41  E-value: 3.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLgYGD-LGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMypgvlVPSSRGG 101
Cdd:PRK13759   7 PNIILIMVDQM-RGDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGR-----VGYGDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LPLEEVTVAEVLAARGYLTGMAGKWHlgVGPEGAFLpphqGFHRFL---GIPYS-HDQGPCQN------LTCFPPATPcd 171
Cdd:PRK13759  81 PWNYKNTLPQEFRDAGYYTQCIGKMH--VFPQRNLL----GFHNVLlhdGYLHSgRNEDKSQFdfvsdyLAWLREKAP-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 172 gGCDQGLVPIPLLANlSVEAQpPWlpGLEARY------MAFAHDLMadaQRQDR--PFFLY--YASHHTHY--PQF---- 235
Cdd:PRK13759 153 -GKDPDLTDIGWDCN-SWVAR-PW--DLEERLhptnwvGSESIEFL---RRRDPtkPFFLKmsFARPHSPYdpPKRyfdm 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 236 -----------SGQSFAERSG---------RGPFGDSLME------------LDAAVGTLMTAIGDLGLLEETLVIFTAD 283
Cdd:PRK13759 225 ykdadipdphiGDWEYAEDQDpeggsidalRGNLGEEYARraraayyglithIDHQIGRFLQALKEFGLLDNTIILFVSD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 284 NGpETMrmsrgGCSGLLRcgKGTTYEGGVREPALAFWPGHIAPG----VTHELASSLDLLPTLAALAGAPLPNvTLDGFD 359
Cdd:PRK13759 305 HG-DML-----GDHYLFR--KGYPYEGSAHIPFIIYDPGGLLAGnrgtVIDQVVELRDIMPTLLDLAGGTIPD-DVDGRS 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 360 LSPLLLGTGKSPRQSL-----FFYPS--YpdevrgvfaVRTGKYKAHFFTQgsahsdttadpachassslTAHEPplLYD 432
Cdd:PRK13759 376 LKNLIFGQYEGWRPYLhgehaLGYSSdnY---------LTDGKWKYIWFSQ-------------------TGEEQ--LFD 425
                        490
                 ....*....|...
gi 313569791 433 LSKDPGENYNLLG 445
Cdd:PRK13759 426 LKKDPHELHNLSP 438
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
22-445 4.35e-34

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: 132.67  E-value: 4.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  22 PPNIVLIFADDLGYGDLGcyghPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpGVLVPSsrGG 101
Cdd:cd16147    1 RPNIVLILTDDQDVELGS----MDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVT-NNSPPG--GG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 LP------LEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGI--PYSHDqgpcqNLTcfppatpcdgg 173
Cdd:cd16147   74 YPkfwqngLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPPGWDEWDGLvgNSTYY-----NYT----------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 174 cdqglvpiplLANLSVEAQPPWLPGlearymAFAHDLMAD--------AQRQDRPFFLYYASH--HTHY---PQFSGQSF 240
Cdd:cd16147  138 ----------LSNGGNGKHGVSYPG------DYLTDVIANkaldflrrAAADDKPFFLVVAPPapHGPFtpaPRYANLFP 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 241 -AERSGRGPFGD---------------------------------SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGP 286
Cdd:cd16147  202 nVTAPPRPPPNNpdvsdkphwlrrlpplnptqiayidelyrkrlrTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGY 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 287 ETmrmsrgGCSGLLRcGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNvTLDgfdlsplllg 366
Cdd:cd16147  282 HL------GQHRLPP-GKRTPYEEDIRVPLLVRGPGIPAGVTVDQLVSNIDLAPTILDLAGAPPPS-DMD---------- 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 367 tGKSPRQSLffYPSYPdevrgvfAVRT--GKYKAHFFtqgsahSDTTADpachasssltaHEpplLYDLSKDPGENYNLL 444
Cdd:cd16147  344 -GRSCGDSN--NNTYK-------CVRTvdDTYNLLYF------EWCTGF-----------RE---LYDLTTDPYQLTNLA 393

                 .
gi 313569791 445 G 445
Cdd:cd16147  394 G 394
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
23-346 1.49e-33

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: 127.15  E-value: 1.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDF-YVPVSLCTPSRAALLTGRLPVRMGMY----PGVLVPS 97
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFNFRsVSPPTSSAPNHAALLTGAYPTLHGYTgngsADPELPS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  98 SRGGLPLEEVTVAEVLAARGYLTGMAGkwhlgvgpegaflpphqgfhrflgipyshdqgpcqnltcfppatpcdggcdqg 177
Cdd:cd00016   81 RAAGKDEDGPTIPELLKQAGYRTGVIG----------------------------------------------------- 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 178 lvpipllanlsveaqppwlpglearymafAHDlMADAQRQDRPFFLYYashhtHYPQFSGQSFAERSGRGPFGDSLMELD 257
Cdd:cd00016  108 -----------------------------LLK-AIDETSKEKPFVLFL-----HFDGPDGPGHAYGPNTPEYYDAVEEID 152
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 258 AAVGTLMTAIGDLGLLEETLVIFTADNGpetmrMSRGGCSGLLR-CGKGTTYEGGVREPALAFWPGHIAPGVTHELASSL 336
Cdd:cd00016  153 ERIGKVLDALKKAGDADDTVIIVTADHG-----GIDKGHGGDPKaDGKADKSHTGMRVPFIAYGPGVKKGGVKHELISQY 227
                        330
                 ....*....|
gi 313569791 337 DLLPTLAALA 346
Cdd:cd00016  228 DIAPTLADLL 237
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-440 1.06e-32

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: 293773 [Multi-domain]  Cd Length: 372  Bit Score: 128.24  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSS--TTPNLDQLAAGGLRFTDFYV-PVslCTPSRAALLTGRLPVRMgmypGVLVPSSR 99
Cdd:cd16154    1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFDNLWAtPA--CSPTRATILTGKYGFRT----GVLAVPDE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 100 GGLPLEEVTVAEVLAAR--GYLTGMAGKWHLGVGPEGafLPPHQGFHRFLGIPYSHDQGPCQ-NLTCFPPATPCDGGCDQ 176
Cdd:cd16154   75 LLLSEETLLQLLIKDATtaGYSSAVIGKWHLGGNDNS--PNNPGGIPYYAGILGGGVQDYYNwNLTNNGQTTNSTEYATT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 177 GLVpipllaNLSVEaqppWLpglearymafahdlmadaQRQDRPFFLYYA-----------SHHTHYPQFSGQSFAERSG 245
Cdd:cd16154  153 KLT------NLAID----WI------------------DQQTKPWFLWLAynaphtpfhlpPAELHSRSLLGDSADIEAN 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 246 RGPFGDSLME-LDAAVGTLMTAIgDLGLLEETLVIFTADNG-PETMR---MSRGGcsgllrcGKGTTYEGGVREPALAFW 320
Cdd:cd16154  205 PRPYYLAAIEaMDTEIGRLLASI-DEEERENTIIIFIGDNGtPGQVVdlpYTRNH-------AKGSLYEGGINVPLIVSG 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 321 PGhIAPGVTHE--LASSLDLLPTLAALAGAPLPNVTlDGFDLSPLLLGTGKSPRQslFFYPSYPDEVRGVFAVRTGKYKA 398
Cdd:cd16154  277 AG-VERANEREsaLVNATDLYATIAELAGVDAAEIH-DSVSFKPLLSDVNASTRQ--YNYTEYESPTTTGWATRNQYYKL 352
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 313569791 399 HFFTQGSAHsdttadpachasssltahepplLYDLSKDPGEN 440
Cdd:cd16154  353 IESENGQEE----------------------LYDLINDPSEQ 372
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
23-453 1.21e-31

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: 126.60  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpssRGGL 102
Cdd:cd16028    1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSV--------WNGT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 PL--EEVTVAEVLAARGYLTGMAGKWHLGVGPEG---------AFLPPHQGFH---RFLGIPYSHDqgPCQNLTcfppat 168
Cdd:cd16028   73 PLdaRHLTLALELRKAGYDPALFGYTDTSPDPRGlapldprllSYELAMPGFDpvdRLDEYPAEDS--DTAFLT------ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 169 pcDGGCD--QGLVPIPLLANLS-VEAQPPWLpgLEARYMAF-----------AHDLMADAQrqDRPFflyYASHHTHYPQ 234
Cdd:cd16028  145 --DRAIEylDERQDEPWFLHLSyIRPHPPFV--APAPYHALydpadvpppirAESLAAEAA--QHPL---LAAFLERIES 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 235 --FSGQSFAERSGRGPFGDSLM--------ELDAAVGTLMTAIGDLGLLEETLVIFTADNGpETMrmsrgGCSGLLrcGK 304
Cdd:cd16028  216 lsFSPGAANAADLDDEEVAQMRatylgliaEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG-EQL-----GDHWLW--GK 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 305 GTTYEGGVREPALAFWPG----HIAPGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLSPLLLG-TGKSPRQSLF--- 376
Cdd:cd16028  288 DGFFDQAYRVPLIVRDPRreadATRGQVVDAFTESVDVMPTILDWLGGEIPHQ-CDGRSLLPLLAGaQPSDWRDAVHyey 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 377 -FYPSYPDEVR----------GVFAVRTGKYK-AHFftqgsahsdttadpachassslTAHePPLLYDLSKDPGENYNLl 444
Cdd:cd16028  367 dFRDVSTRRPQealglspdecSLAVIRDERWKyVHF----------------------AAL-PPLLFDLKNDPGELRDL- 422

                 ....*....
gi 313569791 445 ggvaGATPE 453
Cdd:cd16028  423 ----AADPA 427
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-378 5.38e-30

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: 119.23  E-value: 5.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMY--PGvlvPSSRG 100
Cdd:cd16035    1 PNILLILTDQERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTdtLG---SPMQP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 101 GLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAflpphqgfhrflgipYSHDQGPCQNLTCFppatpcdggcdqglvp 180
Cdd:cd16035   78 LLSPDVPTLGHMLRAAGYYTAYKGKWHLSGAAGGG---------------YKRDPGIAAQAVEW---------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 181 iplLANL--SVEAQPPWL-------PglearymafaHDLMADAQRQDRpfflyYASHHTHYpqfsgqsfaersgrgpfGD 251
Cdd:cd16035  127 ---LRERgaKNADGKPWFlvvslvnP----------HDIMFPPDDEER-----WRRFRNFY-----------------YN 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 252 SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGpetmrmSRGGCSGLLRCGkGTTYEGGVREPAL----AFWPGhiaPG 327
Cdd:cd16035  172 LIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG------EMGGAHGLRGKG-FNAYEEALHVPLIishpDLFGT---GQ 241
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 313569791 328 VTHELASSLDLLPTLAALAGAPLPNV-----TLDGFDLSPLLLGTGKSPRQ--SLFFY 378
Cdd:cd16035  242 TTDALTSHIDLLPTLLGLAGVDAEARateapPLPGRDLSPLLTDADADAVRdgILFTY 299
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-360 3.57e-27

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: 110.54  E-value: 3.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSST----------TPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYP- 91
Cdd:cd16153    2 PNILWIITDDQRVDSLSCYNNAHTGksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGf 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  92 GVLVPSSRGGLPleevTVAEVLAARGYLTGMAGKWHlgvgpegaflppHQGFHRFLGIPYSHDQGPcqnltcfppatpcD 171
Cdd:cd16153   82 EAAHPALDHGLP----TFPEVLKKAGYQTASFGKSH------------LEAFQRYLKNANQSYKSF-------------W 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 172 GGCDQGLVPI-PLLANLSVEA-QPPWLPGLEARymafahdlmadaqrqDRpfFLYYAshhthypqFSGqsfaersgrgpF 249
Cdd:cd16153  133 GKIAKGADSDkPFFVRLSFLQpHTPVLPPKEFR---------------DR--FDYYA--------FCA-----------Y 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 250 GDSLmeldaaVGTLMTAIGDLGLL---EETLVIFTADNGpetmrmSRGGCSGLLrcGKGTTYEGGVREPALAFWPGHI-- 324
Cdd:cd16153  177 GDAQ------VGRAVEAFKAYSLKqdrDYTIVYVTGDHG------WHLGEQGIL--AKFTFWPQSHRVPLIVVSSDKLka 242
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 313569791 325 -APGVTHELASSLDLLPTLAALAGAPLPNVT-LDGFDL 360
Cdd:cd16153  243 pAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDL 280
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
23-445 1.91e-25

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: 108.48  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRlpvrmgmYPGVlvpssRGG- 101
Cdd:cd16150    1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGW-------YPHV-----NGHr 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 102 -----LPLEEVTVAEVLAARGYLTGMAGKWHLGVGP--------------EGA--FL---PPHQGFHRFLGIPYSHdqgp 157
Cdd:cd16150   69 tlhhlLRPDEPNLLKTLKDAGYHVAWAGKNDDLPGEfaaeaycdsdeacvRTAidWLrnrRPDKPFCLYLPLIFPH---- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 158 cqnltcfPPAT---PCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMafahdlmadaQRQDRPFFlyYASHHTHYPQ 234
Cdd:cd16150  145 -------PPYGveePWFSMIDREKLPPRRPPGLRAKGKPSMLEGIEKQGL----------DRWSEERW--RELRATYLGM 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 235 FSgqsfaersgrgpfgdslmELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETmrmsrgGCSGLLRCGKGTTYEGGVRE 314
Cdd:cd16150  206 VS------------------RLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYT------GDYGLVEKWPNTFEDCLTRV 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 315 PALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLdGFDLSPLLLGTGKSPRQSLF----FYPSYPDevrgvfA 390
Cdd:cd16150  262 PLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRDAVFseggRLHGEEQ------A 334
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313569791 391 VRTGKYKAHFFT-QGSAHSDTTADPACHASSSLTA------HEPPLLYDLSKDPGENYNLLG 445
Cdd:cd16150  335 MEGGHGPYDLKWpRLLQQEEPPEHTKAVMIRTRRYkyvyrlYEPDELYDLEADPLELHNLIG 396
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
370-503 2.08e-24

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 98.15  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  370 SPRQSLFFYPSYPdevrgVFAVRTGKYKAHFFTqGSAHSDTtaDPACHASS-SLTAHEPPLLYDLSKDPGENYNLlggvA 448
Cdd:pfam14707   1 SPHEFLFHYCGAA-----LHAVRWGPYKAHFFT-PSFDPPG--AEGCYGSKvPVTHHDPPLLFDLERDPSEKYPL----S 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 313569791  449 GATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGE---DPALQICChPGCtprPACCH 503
Cdd:pfam14707  69 PDSPEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNylwDPWLQPCC-PTF---PACTC 122
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
23-445 5.16e-24

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 104.77  E-value: 5.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSrggl 102
Cdd:cd16156    1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 103 plEEVTVAEVLAARGYLTGMAGKWHL--------GVGPEGaflpphqgfhrflgipyshdqgpcqnltcFPPATPCDGGC 174
Cdd:cd16156   77 --NVKTIGQRLSDNGIHTAYIGKWHLdggdyfgnGICPQG-----------------------------WDPDYWYDMRN 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 175 dqglvpipLLANLSVEAQPPW---LPGLEARYMA----FAHDLMADA-----QRQDRPFFLYYASHHTHYPQFSGQSFAE 242
Cdd:cd16156  126 --------YLDELTEEERRKSrrgLTSLEAEGIKeeftYGHRCTNRAldfieKHKDEDFFLVVSYDEPHHPFLCPKPYAS 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 ----------------------------RSGRGPFGDSL---MEL--------DAAVGTLMTAIGDlgLLEETLVIFTAD 283
Cdd:cd16156  198 mykdfefpkgenayddlenkplhqrlwaGAKPHEDGDKGtikHPLyfgcnsfvDYEIGRVLDAADE--IAEDAWVIYTSD 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 284 NGpETMrmsrgGCSGLLrcGKG-TTYEGGVREPALAFWPGHI-APGVTHELASSLDLLPTLAALAGAPLPNVtLDGFDLS 361
Cdd:cd16156  276 HG-DML-----GAHKLW--AKGpAVYDEITNIPLIIRGKGGEkAGTVTDTPVSHIDLAPTILDYAGIPQPKV-LEGESIL 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 362 PLLLGTGKSPRQSLF---------------FYPsypdeVRGVFavrTGKYK--AHFFTQGSahsdttadpachassslta 424
Cdd:cd16156  347 ATIEDPEIPENRGVFvefgryevdhdgfggFQP-----VRCVV---DGRYKlvINLLSTDE------------------- 399
                        490       500
                 ....*....|....*....|.
gi 313569791 425 hepplLYDLSKDPGENYNLLG 445
Cdd:cd16156  400 -----LYDLEKDPYEMHNLID 415
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
21-360 3.37e-18

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 87.40  E-value: 3.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  21 RPPNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPV--SlctpSRA--ALLTGRLPVRMGmypG 92
Cdd:COG1368  233 KKPNVVVIllesFSDFF----IGALGNGKDVTPFLDSLAKESLYFGNFYSQGgrT----SRGefAVLTGLPPLPGG---S 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  93 VLVPSSRGGLPleevTVAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPa 167
Cdd:COG1368  302 PYKRPGQNNFP----SLPSILKKQGYETsffhgGDGSFWNR-----DSFY-KNLGFDEFYDRED------------FDD- 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 168 tPCDGG---CDQglvpipllanlsveaqppwlpglearymAFAHDLMADAQRQDRPFFLYY--ASHHTHYPQFSGQSFAE 242
Cdd:COG1368  359 -PFDGGwgvSDE----------------------------DLFDKALEELEKLKKPFFAFLitLSNHGPYTLPEEDKKIP 409
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 243 RSGRGPFGD---SLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrMSRGGCSGLLRCGKGTTyeggvrePALaF 319
Cdd:COG1368  410 DYGKTTLNNylnAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGP----RSPGKTDYENPLERYRV-------PLL-I 477
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 313569791 320 W-PGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDL 360
Cdd:COG1368  478 YsPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDL 519
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
23-437 4.45e-18

arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. 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: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 85.67  E-value: 4.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLIFADDLgygDLGCYGHPSSTT---PNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYpgvlvpSSR 99
Cdd:cd16171    1 PNVVMVMSDSF---DGRLTFRPGNQVvdlPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW------NNY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 100 GGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPegaflppHQGFHRFLG----IPYSHDQG--PCQNLTCfppatpcdgg 173
Cdd:cd16171   72 KGLDPNYPTWMDRLEKHGYHTQKYGKLDYTSGH-------HSVSNRVEAwtrdVPFLLRQEgrPTVNLVG---------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 174 cDQGLVPIPLLANLSVEAQPPWLpglearymafahdlMADAQRQDRPFFLYYASHHTH-YP-QFSGQSFAE-RSGRGPFG 250
Cdd:cd16171  135 -DRSTVRVMLKDWQNTDKAVHWI--------------RKEAPNLTQPFALYLGLNLPHpYPsPSMGENFGSiRNIRAFYY 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 251 DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSrggcsgllRCGKGTTYEGGVREPALAFWPGhIAPGVTH 330
Cdd:cd16171  200 AMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHR--------QFYKMSMYEGSSHVPLLIMGPG-IKAGQQV 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 331 ELASSL-DLLPTLAALAGAPLPNvTLDGFDLSPLLLGTGKSPRQSLFFYPSYP-DEVRG------VFAVRTGKYKAHFFT 402
Cdd:cd16171  271 SDVVSLvDIYPTMLDIAGVPQPQ-NLSGYSLLPLLSESSIKESPSRVPHPDWVlSEFHGcnvnasTYMLRTNSWKYIAYA 349
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 313569791 403 QGsahsdttadpachasssltAHEPPLLYDLSKDP 437
Cdd:cd16171  350 DG-------------------NSVPPQLFDLSKDP 365
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
23-347 3.94e-16

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: 78.88  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  23 PNIVLI----FADDLgygdLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRA--ALLTGRLPVRMGmyPGVLVP 96
Cdd:cd16015    1 PNVIVIllesFSDPY----IDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLG--SGSYTL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  97 SSRGGLPleevTVAEVLAARGYLT-----GMAGKWHLgvgpeGAFLpPHQGFHRFLGIPYshdqgpcqnltcFPPATPCD 171
Cdd:cd16015   75 YKLNPLP----SLPSILKEQGYETifihgGDASFYNR-----DSVY-PNLGFDEFYDLED------------FPDDEKET 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 172 GG---CDQGLvpipllanlsveaqppwlpglearyMAFAHDLMADAQRQdrPFFLY---YASHH-----THYPQFSGQSF 240
Cdd:cd16015  133 NGwgvSDESL-------------------------FDQALEELEELKKK--PFFIFlvtMSNHGpydlpEEKKDEPLKVE 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 241 AERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPetmrmsrggcsGLLRCGKGTTYEGGVRE--PALA 318
Cdd:cd16015  186 EDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLP-----------SLGSDYDETDEDPLDLYrtPLLI 254
                        330       340
                 ....*....|....*....|....*....
gi 313569791 319 FWPGHIAPGVTHELASSLDLLPTLAALAG 347
Cdd:cd16015  255 YSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
21-285 7.98e-07

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 51.29  E-value: 7.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  21 RPPNIVLIFADDLGYGDLGcyghpSSTTPNLDQLAAGGLRFTDFYVPV-SLCTPSRAALLTGRLPVRMGM---------Y 90
Cdd:COG1524   22 PAKKVVLILVDGLRADLLE-----RAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIvgngwydpeL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  91 PGVLVPSSRGGLP------LEEVTVAEVLAARGYLTGMAGKWHLGVGP--EGAFLPPHQGFHRFLGIPYShdqgpcqnlt 162
Cdd:COG1524   97 GRVVNSLSWVEDGfgsnslLPVPTIFERARAAGLTTAAVFWPSFEGSGliDAARPYPYDGRKPLLGNPAA---------- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 163 cfppatpcdggcDQGLVpipllanlsveaqppwlpglearymafahDLMADAQRQDRPFFLY-------YASHHThypqf 235
Cdd:COG1524  167 ------------DRWIA-----------------------------AAALELLREGRPDLLLvylpdldYAGHRY----- 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 313569791 236 sgqsfaersgrGPFG----DSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNG 285
Cdd:COG1524  201 -----------GPDSpeyrAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
189-285 3.32e-04

Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.


Pssm-ID: 293742 [Multi-domain]  Cd Length: 267  Bit Score: 42.57  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791 189 VEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYashHTHYPQFSGQSFaersgrGPFG----DSLMELDAAVGTLM 264
Cdd:cd16018  126 IPLGGYWQPYNDSFPFEERVDTILEWLDLERPDLILL---YFEEPDSAGHKY------GPDSpevnEALKRVDRRLGYLI 196
                         90       100
                 ....*....|....*....|.
gi 313569791 265 TAIGDLGLLEETLVIFTADNG 285
Cdd:cd16018  197 EALKERGLLDDTNIIVVSDHG 217
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
209-293 2.75e-03

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 40.10  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313569791  209 DLMADAQRQDRPFFLYYASHHTHYpqfSGQSFAERSGRgpFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPET 288
Cdd:pfam01663 152 DLPFADVAAERPDLLLVYLEEPDY---AGHRYGPDSPE--VEDALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHGMTP 226

                  ....*
gi 313569791  289 MRMSR 293
Cdd:pfam01663 227 VSDDK 231
LptA cd16017
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ...
21-65 6.38e-03

Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.


Pssm-ID: 293741 [Multi-domain]  Cd Length: 288  Bit Score: 38.76  E-value: 6.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 313569791  21 RPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFY 65
Cdd:cd16017    1 KPKNVVLVIGESARRDHMSLYGYPRDTTPFLSKLKKNLIVFDNVI 45
 
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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