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Conserved domains on  [gi|2217392264|ref|XP_047298065|]
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arylsulfatase L isoform X3 [Homo sapiens]

Protein Classification

alkaline phosphatase family protein( domain architecture ID 581061)

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
ALP_like super family cl23718
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
62-398 1.03e-163

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.


The actual alignment was detected with superfamily member cd16159:

Pssm-ID: 474031 [Multi-domain]  Cd Length: 521  Bit Score: 470.62  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGLI----------------------------------------------------- 168
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIgkwhlglhcesrndfchhplnhgfdyfyglpltnlkdcgdgsngeydlsfdpl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16159   161 fplltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfncilmrnhevveqpmslenltqrltke 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 169 ----------------------------------------------------GRILDTLDVEGLSNSTLIYFTSDHGGSL 196
Cdd:cd16159   241 aisflernkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvGQILDALDELGLKDNTFVYFTSDNGGHL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 197 ENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLL 276
Cdd:cd16159   321 EEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLM 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 277 PLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSR 356
Cdd:cd16159   401 PLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSA 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 2217392264 357 DPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16159   480 DPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
62-398 1.03e-163

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: 470.62  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGLI----------------------------------------------------- 168
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIgkwhlglhcesrndfchhplnhgfdyfyglpltnlkdcgdgsngeydlsfdpl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16159   161 fplltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfncilmrnhevveqpmslenltqrltke 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 169 ----------------------------------------------------GRILDTLDVEGLSNSTLIYFTSDHGGSL 196
Cdd:cd16159   241 aisflernkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvGQILDALDELGLKDNTFVYFTSDNGGHL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 197 ENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLL 276
Cdd:cd16159   321 EEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLM 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 277 PLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSR 356
Cdd:cd16159   401 PLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSA 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 2217392264 357 DPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16159   480 DPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
44-362 3.85e-82

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 257.50  E-value: 3.85e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119     5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL------------------------------------ 167
Cdd:COG3119    85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALfgkwhlyltdlltdkaidflerqadkdkpfflylaf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 -------------------------------------------------------IGRILDTLDVEGLSNSTLIYFTSDH 192
Cdd:COG3119   158 naphapyqapeeyldkydgkdiplppnlaprdlteeelrraraayaamieevddqVGRLLDALEELGLADNTIVVFTSDN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 193 GGSLENQlG-----NTQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 266
Cdd:COG3119   238 GPSLGEH-GlrggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 267 DrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhh 346
Cdd:COG3119   300 D--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------ 348
                         410
                  ....*....|....*.
gi 2217392264 347 DPPLLFDLSRDPSETH 362
Cdd:COG3119   349 GPWELYDLKNDPGETN 364
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
286-420 2.69e-60

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 191.76  E-value: 2.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 286 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 365
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217392264 366 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 420
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
PRK13759 PRK13759
arylsulfatase; Provisional
61-369 1.02e-19

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 90.88  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS-------- 131
Cdd:PRK13759    5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGygdvvpwn 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 132 -----------------SIG---------------------------------------YRVLQWTGASG--------GL 147
Cdd:PRK13759   84 ykntlpqefrdagyytqCIGkmhvfpqrnllgfhnvllhdgylhsgrnedksqfdfvsdYLAWLREKAPGkdpdltdiGW 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 148 -----------------PTNET---------------------TFAK--------------------------------- 156
Cdd:PRK13759  164 dcnswvarpwdleerlhPTNWVgsesieflrrrdptkpfflkmSFARphspydppkryfdmykdadipdphigdweyaed 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 157 -------------ILKEK-------GYaTGL-------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ----- 204
Cdd:PRK13759  244 qdpeggsidalrgNLGEEyarraraAY-YGLithidhqIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkg 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 205 --YGGwngiykggkgmggwegGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLL 279
Cdd:PRK13759  319 ypYEG----------------SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLI 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 280 LG-TAQHSDHEFLMH-YCERFLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSR 356
Cdd:PRK13759  381 FGqYEGWRPYLHGEHaLGYSSDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKK 428
                         490
                  ....*....|...
gi 2217392264 357 DPSETHILTPASE 369
Cdd:PRK13759  429 DPHELHNLSPSEK 441
 
Name Accession Description Interval E-value
ES cd16159
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ...
62-398 1.03e-163

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: 470.62  E-value: 1.03e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16159     1 KPNIVLFMADDLGIGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGMASSHGMRVILFT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGLI----------------------------------------------------- 168
Cdd:cd16159    81 ASSGGLPPNETTFAEVLKQQGYSTALIgkwhlglhcesrndfchhplnhgfdyfyglpltnlkdcgdgsngeydlsfdpl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16159   161 fplltafvlitaltiflllylgavskrffvfllilsllfislfflllitnryfncilmrnhevveqpmslenltqrltke 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 169 ----------------------------------------------------GRILDTLDVEGLSNSTLIYFTSDHGGSL 196
Cdd:cd16159   241 aisflernkerpfllvmsflhvhtalftskkfkgrskhgrygdnveemdwsvGQILDALDELGLKDNTFVYFTSDNGGHL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 197 ENQLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLL 276
Cdd:cd16159   321 EEISVGGEYGGGNGGIYGGKKMGGWEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLPSDRIIDGRDLM 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 277 PLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFVTPVFQPEGAGaCYGRKVCPCFGEKVVHHDPPLLFDLSR 356
Cdd:cd16159   401 PLLTGQEKRSPHEFLFHYCGAELHAVRYRPRDGGAVWKAHYFTPNFYPGTEG-CCGTLLCRCFGDSVTHHDPPLLFDLSA 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 2217392264 357 DPSETHILTPASEPvFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16159   480 DPSESNPLDPTDEP-YQEIIKKILEAVAEHQSSIEPVESQLS 520
GALNS_like cd16026
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
62-362 8.98e-96

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: 292.93  E-value: 8.98e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRVLQWT 141
Cdd:cd16026     1 KPNIVVILADDLGYGDLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGL-----PGVVGPP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16026    76 GSKGGLPPDEITIAEVLKKAGYRTALVGkwhlghqpeflptrhgfdeyfgipysndmwpfplyrndppgplpplmeneev 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 ----------------------------------------------------------------------RILDTLDVEG 179
Cdd:cd16026   156 ieqpadqssltqrytdeavdfiernkdqpfflylahtmphvplfasekfkgrsgaglygdvveeldwsvgRILDALKELG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 180 LSNSTLIYFTSD---------HGGSleNQL-----GNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGE 245
Cdd:cd16026   236 LEENTLVIFTSDngpwleyggHGGS--AGPlrggkGTTWEGG-----------------VRVPFIAWWPGVIPAGTVSDE 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 246 PTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPE 325
Cdd:cd16026   297 LASTMDLLPTLAALAGAPLPEDRVIDGKDISPLLLGGSKSPPHPFFYYYDGGDLQAVRSGR------WKLHLPTTYRTGT 370
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2217392264 326 GAGacygrkvcpcfGEKVVHHDPPLLFDLSRDPSETH 362
Cdd:cd16026   371 DPG-----------GLDPTKLEPPLLYDLEEDPGETY 396
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
44-362 3.85e-82

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 257.50  E-value: 3.85e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRY 123
Cdd:COG3119     5 LLLLLALLAAAAAAAAAKRPNILFILADDLGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 124 PVRSGMVSSIGyrvlqwtGASGGLPTNETTFAKILKEKGYATGL------------------------------------ 167
Cdd:COG3119    85 PHRTGVTDNGE-------GYNGGLPPDEPTLAELLKEAGYRTALfgkwhlyltdlltdkaidflerqadkdkpfflylaf 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 -------------------------------------------------------IGRILDTLDVEGLSNSTLIYFTSDH 192
Cdd:COG3119   158 naphapyqapeeyldkydgkdiplppnlaprdlteeelrraraayaamieevddqVGRLLDALEELGLADNTIVVFTSDN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 193 GGSLENQlG-----NTQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQ 266
Cdd:COG3119   238 GPSLGEH-GlrggkGTLYeGG-----------------IRVPLIVRWPGKIKAGSVSDALVSLIDLLPTLLDLAGVPIPE 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 267 DrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRdrgtmWKVHFvtpvfqpegagaCYGRKvcpcfgekvvhh 346
Cdd:COG3119   300 D--LDGRSLLPLLTGEKAEWRDYLYWEYPRGGGNRAIRTGR-----WKLIR------------YYDDD------------ 348
                         410
                  ....*....|....*.
gi 2217392264 347 DPPLLFDLSRDPSETH 362
Cdd:COG3119   349 GPWELYDLKNDPGETN 364
ARS_like cd16142
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-365 5.32e-72

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: 230.88  E-value: 5.32e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYG---NNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssigYRVlQ 139
Cdd:cd16142     1 PNILVILGDDIGWGDLGCYGggiGRGAPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHPIRTGL-----TTV-G 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 140 WTGASGGLPTNETTFAKILKEKGYATGL---------------------------------------------------- 167
Cdd:cd16142    74 LPGSPGGLPPWEPTLAELLKDAGYATAQfgkwhlgdedgrlptdhgfdefygnlyhtideeivdkaidfikrnakadkpf 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 ---------------------------------------IGRILDTLDVEGLSNSTLIYFTSDHG-----------GSLE 197
Cdd:cd16142   154 flyvnftkmhfptlpspefegkssgkgkyadsmvelddhVGQILDALDELGIADNTIVIFTTDNGpeqdvwpdggyTPFR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 198 NQLGNTQYGGWngiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVP------QDRVID 271
Cdd:cd16142   234 GEKGTTWEGGV-----------------RVPAIVRWPGKIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgKDRHID 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 272 GQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVtpVFQPEGAGACYGRKVCPCfgekvvhhdpPLL 351
Cdd:cd16142   297 GVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKN------WKVHFK--AQEDTGGPTGEPFYVLTF----------PLI 358
                         410
                  ....*....|....
gi 2217392264 352 FDLSRDPSETHILT 365
Cdd:cd16142   359 FNLRRDPKERYDVT 372
spARS_like cd16160
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ...
62-379 6.07e-72

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: 233.09  E-value: 6.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSsiGYRV-LQW 140
Cdd:cd16160     1 KPNIVLFFADDMGYGDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYG--GTRVfLPW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 141 TgaSGGLPTNETTFAKILKEKGYATGLIGR-------------------------------------------------- 170
Cdd:cd16160    79 D--IGGLPKTEVTMAEALKEAGYTTGMVGKwhlginennhsdgahlpshhgfdfvgtnlpftnswacddtgrhvdfpdrs 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16160   157 acflyyndtiveqpiqhehltetlvgdaksfiednqenpfflyfsfpqthtplfaskrfkgkskrgrygdninemswavg 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 171 -ILDTLDVEGLSNSTLIYFTSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVL 237
Cdd:cd16160   237 eVLDTLVDTGLDQNTLVFFLSDHGphveycleggstGGLKGGKGNSWEGG-----------------IRVPFIAYWPGTI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 238 PaGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERfLHAARWHQrdrgtmWKVHF 317
Cdd:cd16160   300 K-PRVSHEVVSTMDIFPTFVDLAGGTLPTDRIYDGLSITDLLLGEADSPHDDILYYCCSR-LMAVRYGS------YKIHF 371
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217392264 318 VT---PVFQPEGAGACYGRKVCP------CFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMERV 379
Cdd:cd16160   372 KTqplPSQESLDPNCDGGGPLSDyivcydCEDECVTKHNPPLIFDVEKDPGEQYPLQPSVYEHMLEAVEKL 442
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
63-274 1.19e-71

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: 225.39  E-value: 1.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGmvssigyrVLQWTG 142
Cdd:cd16022     1 PNILLIMTDDLGYDDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHG--------VRGNVG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGGLPTNETTFAKILKEKGYATGL----------------------------------------------IGRILDTLD 176
Cdd:cd16022    73 NGGGLPPDEPTLAELLKEAGYRTALigkwhdeaidfierrdkdkpfflyvsfnaphppfayyamvsaiddqIGRILDALE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 177 VEGLSNSTLIYFTSDHGGSLENqlGNTQYGGWNgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTV 256
Cdd:cd16022   153 ELGLLDNTLIVFTSDHGDMLGD--HGLRGKKGS----------LYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTL 220
                         250
                  ....*....|....*...
gi 2217392264 257 VRLAGGEVPQDrvIDGQD 274
Cdd:cd16022   221 LDLAGIEPPEG--LDGRS 236
Sulfatase_C pfam14707
C-terminal region of aryl-sulfatase;
286-420 2.69e-60

C-terminal region of aryl-sulfatase;


Pssm-ID: 405407 [Multi-domain]  Cd Length: 122  Bit Score: 191.76  E-value: 2.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 286 SDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVTPVFQPEGAGACYGRKVCpcfgekVVHHDPPLLFDLSRDPSETHILT 365
Cdd:pfam14707   1 SPHEFLFHYCGAALHAVRWGP------YKAHFFTPSFDPPGAEGCYGSKVP------VTHHDPPLLFDLERDPSEKYPLS 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217392264 366 PASePVFYQVMERVQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWC 420
Cdd:pfam14707  69 PDS-PEYPEVLAEIKAAVEEHKATLVPVPNQLSKGNYLWDPWLQPCCPTFPACTC 122
ARSG cd16161
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ...
62-365 8.38e-60

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: 199.62  E-value: 8.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGN-NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRvlqw 140
Cdd:cd16161     1 KPNFLLLFADDLGWGDLGANWApNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPT---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 141 tgASGGLPTNETTFAKILKEKGYATG------------------------------------------------------ 166
Cdd:cd16161    77 --SVGGLPLNETTLAEVLRQAGYATGmigkwhlgqreaylpnsrgfdyyfgipfshdssladryaqfatdfiqrasakdr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 167 ----------------------------------------LIGRILDTLDVEGLSNSTLIYFTSDHG-----GSLENQLG 201
Cdd:cd16161   155 pfflyaalahvhvplanlprfqsptsgrgpygdalqemddLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkCELAVGPG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 202 NTQY---GGWNGIYKGGKGMGgweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPL 278
Cdd:cd16161   235 TGDWqgnLGGSVAKASTWEGG-----HREPAIVYWPGRIPANSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSPV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 279 LLGTAQhSDHEFLMHYCE-----RFLHAARWHQrdrgtmWKVHFVTpvfqpEGAGACygrkvCPCFGEKvVHHDPPLLFD 353
Cdd:cd16161   310 LFGGSK-TGHRCLFHPNSgaagaGALSAVRCGD------YKAHYAT-----GGALAC-----CGSTGPK-LYHDPPLLFD 371
                         410
                  ....*....|..
gi 2217392264 354 LSRDPSETHILT 365
Cdd:cd16161   372 LEVDPAESFPLT 383
ARS_like cd16144
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-362 8.82e-60

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: 200.46  E-value: 8.82e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16144     1 PNIVLILVDDLGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 A-------SGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------- 169
Cdd:cd16144    81 TklipppsTTRLPLEEVTIAEALKDAGYATAHFGkwhlggeggygpedqgfdvniggtgnggppsyyfppgkpnpdledg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 -----------------------------------------------------------------------------RIL 172
Cdd:cd16144   161 pegeyltdrltdeaidfieqnkdkpfflylshyavhtpiqarpeliekyekkkkglrkgqknpvyaamiesldesvgRIL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 173 DTLDVEGLSNSTLIYFTSDHGG-SLENQLGNTQY-----------GGwngiykggkgmggweggIRVPGIFRWPGVLPAG 240
Cdd:cd16144   241 DALEELGLADNTLVIFTSDNGGlSTRGGPPTSNAplrggkgslyeGG-----------------IRVPLIVRWPGVIKPG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 241 RVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYcerFLHAARWHQRDRGTM----WK-V 315
Cdd:cd16144   304 SVSDVPVIGTDLYPTFLELAGGPLPPPQHLDGVSLVPLLKGGEADLPRRALFWH---FPHYHGQGGRPASAIrkgdWKlI 380
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2217392264 316 HFvtpvfqpegagacygrkvcpcfgekvvHHDPPL-LFDLSRDPSETH 362
Cdd:cd16144   381 EF---------------------------YEDGRVeLYNLKNDIGETN 401
ARSA cd16158
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ...
63-420 1.21e-57

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: 196.51  E-value: 1.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYrvlqwTG 142
Cdd:cd16158     2 PNIVLLFADDLGYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFY-----PG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGGLPTNETTFAKILKEKGYATGLIGR---------------------------------------------------- 170
Cdd:cd16158    77 SRGGLPLNETTIAEVLKTVGYQTAMVGKwhlgvglngtylpthqgfdhylgipyshdqgpcqnltcfppnipcfggcdqg 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16158   157 evpcplfynesivqqpvdlltleeryakfakdfiadnakegkpfflyyashhthypqfagqkfagrssrgpfgdalaeld 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 171 -----ILDTLDVEGLSNSTLIYFTSDHG------------GSLENQLGNTQYGGwngiykggkgmggweggIRVPGIFRW 233
Cdd:cd16158   237 gsvgeLLQTLKENGIDNNTLVFFTSDNGpstmrksrggnaGLLKCGKGTTYEGG-----------------VREPAIAYW 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 234 PGVLPAGRVIgEPTSLMDVFPTVVRLAGGEVPqDRVIDGQDLLPLLLGTAQHSDHEFLMHYC----ERFLHAARWHQrdr 309
Cdd:cd16158   300 PGRIKPGVTH-ELASTLDILPTIAKLAGAPLP-NVTLDGVDMSPILFEQGKSPRQTFFYYPTspdpDKGVFAVRWGK--- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 310 gtmWKVHFVT---PVFQPEGAGACYGRKvcpcfgeKVVHHDPPLLFDLSRDPSETHILTpaSEPVFYQVMERVQQAVWEH 386
Cdd:cd16158   375 ---YKAHFYTqgaAHSGTTPDKDCHPSA-------ELTSHDPPLLFDLSQDPSENYNLL--GLPEYNQVLKQIQQVKERF 442
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 2217392264 387 QRTLSPVPLQLDRLGNiwrPWLQPC----CGPFPLCWC 420
Cdd:cd16158   443 EASMKFGESEINKGED---PALEPCckpgCTPKPSCCQ 477
ARS_like cd16143
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-362 2.98e-54

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: 185.10  E-value: 2.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYG-NNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssiGYRVLQWT 141
Cdd:cd16143     1 PNIVIILADDLGYGDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL----KGGVLGGF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGgLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16143    77 SPPL-IEPDRVTLAKMLKQAGYRTAMVGkwhlgldwkkkdgkkaatgtgkdvdyskpikggpldhgfdyyfgipasevlp 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 ------------------------------------------------------------RILDTLDVEGLSNSTLIYFT 189
Cdd:cd16143   156 tltdkavefidqhakkdkpfflyfalpaphtpivpspefqgksgagpygdfvyeldwvvgRILDALKELGLAENTLVIFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 190 SDHGGSLENQLGNTQ-----------------Y-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMD 251
Cdd:cd16143   236 SDNGPSPYADYKELEkfghdpsgplrgmkadiYeGG-----------------HRVPFIVRWPGKIPAGSVSDQLVSLTD 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 252 VFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHycerflHAARWHQRDRGTMWKVhfvtpVFQPEGAGACY 331
Cdd:cd16143   299 LFATLAAIVGQKLPDNAAEDSFSFLPALLGPKKQEVRESLVH------HSGNGSFAIRKGDWKL-----IDGTGSGGFSY 367
                         410       420       430
                  ....*....|....*....|....*....|..
gi 2217392264 332 GRKvcpcfgeKVVHHDPP-LLFDLSRDPSETH 362
Cdd:cd16143   368 PRG-------KEKLGLPPgQLYNLSTDPGESN 392
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
63-388 5.98e-50

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: 173.08  E-value: 5.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIgDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssIGYRVLQWTg 142
Cdd:cd16027     1 PNILWIIADDLSP-DLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGA---HGLRSRGFP- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 asggLPTNETTFAKILKEKGYATGL------------------------------------------------------- 167
Cdd:cd16027    76 ----LPDGVKTLPELLREAGYYTGLigkthynpdavfpfddemrgpddggrnawdyasnaadflnrakkgqpfflwfgfh 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 --------------------------------------------------IGRILDTLDVEGLSNSTLIYFTSDHGGSLE 197
Cdd:cd16027   152 dphrpyppgdgeepgydpekvkvppylpdtpevredladyydeierldqqVGEILDELEEDGLLDNTIVIFTSDHGMPFP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 198 NQLGNTQYGGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLP 277
Cdd:cd16027   232 RAKGTLYDSG-----------------LRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLLDLAGIEPPEY--LQGRSFLP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 278 LLLG-TAQHSDHEFLMH-------YCERFLHAARWHqrdrgtmwkvhfvtpvfqpegagacYgrkvcpcfgekVVHHDPP 349
Cdd:cd16027   293 LLKGeKDPGRDYVFAERdrhdetyDPIRSVRTGRYK-------------------------Y-----------IRNYMPE 336
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2217392264 350 LLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWEHQR 388
Cdd:cd16027   337 ELYDLKNDPDELNNL--ADDPEYAEVLEELRAALDAWMK 373
GALNS cd16157
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ...
62-398 1.10e-49

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: 174.96  E-value: 1.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWT 141
Cdd:cd16157     1 KPNIILMLMDDMGWGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GAS--GGLPTNETTFAKILKEKGYATGLIGR------------------------------------------------- 170
Cdd:cd16157    81 PQNivGGIPDSEILLPELLKKAGYRNKIVGKwhlghrpqyhplkhgfdewfgapnchfgpydnkaypnipvyrdwemigr 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 171 -------------------------------------------------------------------------------I 171
Cdd:cd16157   161 yyeefkidkktgesnltqiylqealefiekqhdaqkpfflywapdathapvyaskpflgtsqrglygdavmeldssvgkI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 172 LDTLDVEGLSNSTLIYFTSDHGGSLenqLGNTQYGGWNGIYKGGKGMGGWEGgIRVPGIFRWPGVLPAGRVIGEPTSLMD 251
Cdd:cd16157   241 LESLKSLGIENNTFVFFSSDNGAAL---ISAPEQGGSNGPFLCGKQTTFEGG-MREPAIAWWPGHIKPGQVSHQLGSLMD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 252 VFPTVVRLAGGEVPQDRVIDGQDLLPLLLgtAQHSDHEFLMHYCERFLHAARWHQrdrgtmWKVHFVT----PVFQPEGA 327
Cdd:cd16157   317 LFTTSLALAGLPIPSDRAIDGIDLLPVLL--NGKEKDRPIFYYRGDELMAVRLGQ------YKAHFWTwsnsWEEFRKGI 388
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217392264 328 GACYGRKVCPCFGEKVVHH-DPPLLFDLSRDPSETHILTPASePVFYQVMERVQQAVWEHQRTLSPVPLQLD 398
Cdd:cd16157   389 NFCPGQNVPGVTTHNQTDHtKLPLLFHLGRDPGEKYPISFKS-AEYKQAMPRISKVVQQHQKTLVPGEPQLN 459
ARS_like cd16146
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ...
63-385 2.34e-49

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: 172.73  E-value: 2.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HISaaSLCTPSRAAFLTGRYPVRSGMVSSIGYRVLqwt 141
Cdd:cd16146     1 PNVILILTDDQGYGDLGFHGNPILKTPNLDRLAAESVRFTNfHVS--PVCAPTRAALLTGRYPFRTGVWHTILGRER--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 gasggLPTNETTFAKILKEKGYATGL------------------------------------------------------ 167
Cdd:cd16146    76 -----MRLDETTLAEVFKDAGYRTGIfgkwhlgdnypyrpqdrgfdevlghggggigqypdywgndyfddtyyhngkfvk 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 ----------------------------------------------------------------------IGRILDTLDV 177
Cdd:cd16146   151 tegyctdvffdeaidfieenkdkpffaylatnaphgplqvpdkyldpykdmglddklaafygmieniddnVGRLLAKLKE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 178 EGLSNSTLIYFTSDHGGSLENQLGN---------TQY-GGwngiykggkgmggweggIRVPGIFRWPGVLPAGRVIGEPT 247
Cdd:cd16146   231 LGLEENTIVIFMSDNGPAGGVPKRFnagmrgkkgSVYeGG-----------------HRVPFFIRWPGKILAGKDVDTLT 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 248 SLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerFLHaarWHQRDRGTMWKVHFVtpVFQPEga 327
Cdd:cd16146   294 AHIDLLPTLLDLCGVKLPEGIKLDGRSLLPLLKGESDPWPERTL------FTH---SGRWPPPPKKKRNAA--VRTGR-- 360
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217392264 328 gacYgRKVCPcfgekvvHHDPPLLFDLSRDPSETHILTpASEPVFYQVMERVQQAVWE 385
Cdd:cd16146   361 ---W-RLVSP-------KGFQPELYDIENDPGEENDVA-DEHPEVVKRLKAAYEAWWD 406
ARS_like cd16145
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ...
63-362 6.91e-49

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: 171.62  E-value: 6.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyRVLQWTG 142
Cdd:cd16145     1 PNIIFILADDLGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRV------RGNSEPG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGGLPTNETTFAKILKEKGYATGLIG----------------------------------------------------- 169
Cdd:cd16145    75 GQDPLPPDDVTLAEVLKKAGYATAAFGkwglggpgtpghptkqgfdyfygyldqvhahnyypeylwrngekvplpnnvip 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16145   155 pldegnnagggggtyshdlftdealdfirenkdkpfflylaytlphaplqvpddgpykykpkdpgiyaylpwpqpekaya 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 -----------RILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQY--------------------GGwngiykggkgm 218
Cdd:cd16145   235 amvtrldrdvgRILALLKELGIDENTLVVFTSDNGPHSE---GGSEHdpdffdsngplrgykrslyeGG----------- 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 219 ggweggIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLmhYCERF 298
Cdd:cd16145   301 ------IRVPFIARWPGKIPAGSVSDHPSAFWDFMPTLADLAGAEPPED--IDGISLLPTLLGKPQQQQHDYL--YWEFY 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217392264 299 LH----AARWHQrdrgtmWKVhfvtpVFQPEGAGacygrkvcpcfgekvvhhdPPLLFDLSRDPSETH 362
Cdd:cd16145   371 EGggaqAVRMGG------WKA-----VRHGKKDG-------------------PFELYDLSTDPGETN 408
PAS_like cd16025
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ...
62-362 6.77e-45

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: 160.69  E-value: 6.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNtMRTPNIDRLAEDGVKLTQ-HisAASLCTPSRAAFLTGRYPVRSGMvSSIGYRVLQW 140
Cdd:cd16025     2 RPNILLILADDLGFSDLGCFGGE-IPTPNLDALAAEGLRFTNfH--TTALCSPTRAALLTGRNHHQVGM-GTMAELATGK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 141 TGASGGLPTNETTFAKILKEKGYAT------------------------------------------------------- 165
Cdd:cd16025    78 PGYEGYLPDSAATIAEVLKDAGYHTymsgkwhlgpddyystddltdkaieyideqkapdkpfflylafgaphaplqapke 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 166 ---------------------------GL---------------------------------------------IGRILD 173
Cdd:cd16025   158 widkykgkydagwdalreerlerqkelGLipadtkltprppgvpawdslspeekklearrmevyaamvehmdqqIGRLID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 174 TLDVEGLSNSTLIYFTSDHGGSLEN---QLGNTQY---------GGwngiykggkgmggweggIRVPGIFRWP-GVLPAG 240
Cdd:cd16025   238 YLKELGELDNTLIIFLSDNGASAEPgwaNASNTPFrlykqasheGG-----------------IRTPLIVSWPkGIKAKG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 241 RVIGEPTSLMDVFPTVVRLAGGEVPQDRV------IDGQDLLPLLLGTAQHSDHEFLmhYCERFLHAARWHQRdrgtmWK 314
Cdd:cd16025   301 GIRHQFAHVIDIAPTILELAGVEYPKTVNgvpqlpLDGVSLLPTLDGAAAPSRRRTQ--YFELFGNRAIRKGG-----WK 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217392264 315 VhfvtpvfqpegagacygrkvcpcfgekVVHHDPPL------LFDLSRDPSETH 362
Cdd:cd16025   374 A---------------------------VALHPPPGwgdqweLYDLAKDPSETH 400
sulfatase_like cd16149
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-277 5.59e-43

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: 151.62  E-value: 5.59e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTG 142
Cdd:cd16149     1 PNILFILTDDQGPWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKTK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGGLPTNETTFAKILKEKGYATGL-------------------------------------------------IGRILD 173
Cdd:cd16149    81 KPEGYLEGQTTLPEVLQDAGYRCGLsgkwhlgddaadflrrraeaekpfflsvnytaphspwgyfaavtgvdrnVGRLLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 174 TLDVEGLSNSTLIYFTSDHGGSLenqlgnTQYGGW---------NgiykggkgmgGWEGGIRVPGIFRWPGVLPAGRVIG 244
Cdd:cd16149   161 ELEELGLTENTLVIFTSDNGFNM------GHHGIWgkgngtfplN----------MYDNSVKVPFIIRWPGVVPAGRVVD 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2217392264 245 EPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLP 277
Cdd:cd16149   225 SLVSAYDFFPTLLELAGVDPPADPRLPGRSFAD 257
sulfatase_like cd16151
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-304 4.33e-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: 293770 [Multi-domain]  Cd Length: 377  Bit Score: 152.37  E-value: 4.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqwtg 142
Cdd:cd16151     1 PNIILIMADDLGYECIGCYGGESYKTPNIDALAAEGVRFN-NAYAQPLCTPSRVQLMTGKYNFRNYVV------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 aSGGLPTNETTFAKILKEKGYATG-------------------------------------------------------- 166
Cdd:cd16151    68 -FGYLDPKQKTFGHLLKDAGYATAiagkwqlgggrgdgdyphefgfdeyclwqltetgekysrpatptfnirngkllett 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 167 ----------------------------------------------------------------------LIGRILDTLD 176
Cdd:cd16151   147 egdygpdlfadflidfiernkdqpffayypmvlvhdpfvptpdspdwdpddkrkkddpeyfpdmvaymdkLVGKLVDKLE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 177 VEGLSNSTLIYFTSDHG--GSLENQLGNTQY-GGwngiykggkGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVF 253
Cdd:cd16151   227 ELGLRENTIIIFTGDNGthRPITSRTNGREVrGG---------KGKTTDAGTHVPLIVNWPGLIPAGGVSDDLVDFSDFL 297
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217392264 254 PTVVRLAGGEVPQDRVIDGQDLLPLLLG-TAQHSDHEFLMHY-------CERFLHAARW 304
Cdd:cd16151   298 PTLAELAGAPLPEDYPLDGRSFAPQLLGkTGSPRREWIYWYYrnphkkfGSRFVRTKRY 356
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-358 2.59e-40

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: 146.15  E-value: 2.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRsgmvssIGYrvlqWTG 142
Cdd:cd16037     1 PNILIIMSDEHNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHE------TGV----WDN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASgGLPTNETTFAKILKEKGYAT--------------------------------------------------------- 165
Cdd:cd16037    71 AD-PYDGDVPSWGHALRAAGYETvligklhfrgedqrhgfrydrdvteaavdwlreeaaddkpwflfvgfvaphfpliap 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 166 ----------------GL-------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLG-------NTQYggwngiykgg 215
Cdd:cd16037   150 qefydlyvrraraayyGLvefldenIGRVLDALEELGLLDNTLIIYTSDHG----DMLGerglwgkSTMY---------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 216 kgmggwEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRviDGQDLLPLLLGTAQHSDHEFlmhyC 295
Cdd:cd16037   216 ------EESVRVPMIISGPGI-PAGKRVKTPVSLVDLAPTILEAAGAPPPPDL--DGRSLLPLAEGPDDPDRVVF----S 282
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217392264 296 ErfLHAARwhQRDRGTM-----WK-VHFVtpvfqpegagacygrkvcpcfgekvvhHDPPLLFDLSRDP 358
Cdd:cd16037   283 E--YHAHG--SPSGAFMlrkgrWKyIYYV---------------------------GYPPQLFDLENDP 320
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
63-358 5.16e-39

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: 142.72  E-value: 5.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16032     1 PNILLIMADQLTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGA----------YDN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGgLPTNETTFAKILKEKGYATGL------------------------------------------------------- 167
Cdd:cd16032    71 AAE-FPADIPTFAHYLRAAGYRTALsgkmhfvgpdqlhgfdydeevafkavqklydlargedgrpffltvsfthphdpyv 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 ---------------------------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGntQYGGWngiykggKGMGG 220
Cdd:cd16032   150 ipqeywdlyvrrarrayygmvsyvddkVGQLLDTLERTGLADDTIVIFTSDHG----DMLG--ERGLW-------YKMSF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 221 WEGGIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRV-IDGQDLLPLLLGTAQHSDHEFLMHYCErfl 299
Cdd:cd16032   217 FEGSARVPLIISAPG-RFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVPpLDGRSLLPLLEGGDSGGEDEVISEYLA--- 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217392264 300 haarwhqrdrgtmwkvhfvtpvfqpEGAGAcygrkvcPCF-----GEKVVH--HDPPLLFDLSRDP 358
Cdd:cd16032   293 -------------------------EGAVA-------PCVmirrgRWKFIYcpGDPDQLFDLEADP 326
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-364 2.58e-38

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: 142.71  E-value: 2.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVsSIGYRvlqwt 141
Cdd:cd16034     1 KPNILFIFADQHRAQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVF-GNDVP----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 gasggLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16034    75 -----LPPDAPTIADVLKDAGYRTGYIGkwhldgperndgraddytppperrhgfdywkgyecnhdhnnphyydddgkri 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16034   150 yikgyspdaetdlaieylenqadkdkpfalvlswnpphdpyttapeeyldmydpkklllrpnvpedkkeeaglredlrgy 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 ------------RILDTLDVEGLSNSTLIYFTSDHG---GSLENQLGNTQYGGwngiykggkgmggwegGIRVPGIFRWP 234
Cdd:cd16034   230 yamitalddnigRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMNKQVPYEE----------------SIRVPFIIRYP 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 235 GVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTM-- 312
Cdd:cd16034   294 GKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT--VEGRDLSPLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGVrt 371
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217392264 313 --WKvhFVtpvfqpegagacygrkvcpcfgekVVHHDPPLLFDLSRDPSETHIL 364
Cdd:cd16034   372 drYT--YV------------------------RDKNGPWLLFDNEKDPYQLNNL 399
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-277 3.50e-38

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: 139.22  E-value: 3.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLgIGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPvrsgmvssigyrvLQWT 141
Cdd:cd16148     1 MNVILIVIDSL-RADhLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP-------------FYHG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGL------------------------------------------------------ 167
Cdd:cd16148    67 VWGGPLEPDDPTLAEILRKAGYYTAAvssnphlfggpgfdrgfdtfedfrgqegdpgeegderaervtdralewldrnad 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 -----------------------------IGRILDTLDVEGLSNSTLIYFTSDHGGSLeNQLGNTQYGGWNgiykggkgm 218
Cdd:cd16148   147 ddpfflflhyfdphepylydaevryvdeqIGRLLDKLKELGLLEDTLVIVTSDHGEEF-GEHGLYWGHGSN--------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217392264 219 gGWEGGIRVPGIFRWPGVLPAGRvIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLP 277
Cdd:cd16148   217 -LYDEQLHVPLIIRWPGKEPGKR-VDALVSHIDIAPTLLDLLGVEPPDY--SDGRSLLP 271
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
61-381 5.85e-38

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: 142.28  E-value: 5.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVssigyrvlqw 140
Cdd:cd16031     1 KRPNIIFILTDDHRYDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVT---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 141 TGASGGLPTNETTFAKILKEKGYATGLIG--------------------------------------------------- 169
Cdd:cd16031    71 DNNGPLFDASQPTYPKLLRKAGYQTAFIGkwhlgsggdlpppgfdywvsfpgqgsyydpefiengkrvgqkgyvtdiitd 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16031   151 kaldflkerdkdkpfclslsfkaphrpftpaprhrglyedvtipepetfddddyagrpewareqrnrirgvldgrfdtpe 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 ---------------------RILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGG-WNgiykggkgmgGWEGGIRV 227
Cdd:cd16031   231 kyqrymkdylrtvtgvddnvgRILDYLEEQGLADNTIIIYTSDNG----FFLGEHGLFDkRL----------MYEESIRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 228 PGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHS-DHEFLMHYCE--RFLHAARW 304
Cdd:cd16031   297 PLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPED--MQGRSLLPLLEGEKPVDwRKEFYYEYYEepNFHNVPTH 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 305 H--QRDRgtmWK-VHFvtpvfqpegagacygrkvcpcfgekvvHHDPPL--LFDLSRDPSETH--ILTPASEPVFYQVME 377
Cdd:cd16031   375 EgvRTER---YKyIYY---------------------------YGVWDEeeLYDLKKDPLELNnlANDPEYAEVLKELRK 424

                  ....
gi 2217392264 378 RVQQ 381
Cdd:cd16031   425 RLEE 428
4-S cd16029
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ...
63-362 1.99e-37

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: 140.38  E-value: 1.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASlCTPSRAAFLTGRYPVRSGMvssiGYRVLqWTG 142
Cdd:cd16029     1 PHIVFILADDLGWNDVGFHGSDQIKTPNLDALAADGVILNNYYVQPI-CTPSRAALMTGRYPIHTGM----QHGVI-LAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 ASGGLPTNETTFAKILKEKGYATGLIG----------------------------------------------------- 169
Cdd:cd16029    75 EPYGLPLNETLLPQYLKELGYATHLVGkwhlgfytweytptnrgfdsfygyyggaedyythtsggandygnddlrdneep 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264     --------------------------------------------------------------------------------
Cdd:cd16029   155 awdyngtystdlftdravdiienhdpskplflylafqavhaplqvppeyadpyedkfahikdedrrtyaamvsaldesvg 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 RILDTLDVEGLSNSTLIYFTSDHGGSLENQLG----------NTQY-GGwngiykggkgmggweggIRVPGiFRWPGVLP 238
Cdd:cd16029   235 NVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyplrggkNTLWeGG-----------------VRVPA-FVWSPLLP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 239 --AGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLmhycerflhaarwHQRDRgtmwkvh 316
Cdd:cd16029   297 pkRGTVSDGLMHVTDWLPTLLSLAGGDPDDLPPLDGVDQWDALSGGAPSPRTEIL-------------LNIDD------- 356
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2217392264 317 fvtPVFQPEGAGACYGRKvcpcfgeKVVHHDPplLFDLSRDPSETH 362
Cdd:cd16029   357 ---ITRTTGGAAIRVGDW-------KLIVGKP--LFNIENDPCERN 390
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-385 4.12e-34

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: 131.57  E-value: 4.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqWTG 142
Cdd:cd16033     1 PNILFIMTDQQRYDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVE-----NAG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 A-SGGLPTNETTFAKILKEKGYATG------------------------------------------------------- 166
Cdd:cd16033    76 AySRGLPPGVETFSEDLREAGYRNGyvgkwhvgpeetpldygfdeylpvettieyfladraiemleelaaddkpfflrvn 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 167 -------------------------------------------------------------------------LIGRILD 173
Cdd:cd16033   156 fwgphdpyippepyldmydpediplpesfaddfedkpyiyrrerkrwgvdtedeedwkeiiahywgyitliddAIGRILD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 174 TLDVEGLSNSTLIYFTSDHGGSLENQlgntqyGGWNGIYKGGKGMGgweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVF 253
Cdd:cd16033   236 ALEELGLADDTLVIFTSDHGDALGAH------RLWDKGPFMYEETY------RIPLIIKWPGVIAAGQVVDEFVSLLDLA 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 254 PTVVRLAGGEVPQDrvIDGQDLLPLLLGT----------AQHSDHEFLmhYCERFLHAARWHQrdrgtmwkvhfvtpVFQ 323
Cdd:cd16033   304 PTILDLAGVDVPPK--VDGRSLLPLLRGEqpedwrdevvTEYNGHEFY--LPQRMVRTDRYKY--------------VFN 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217392264 324 PEGagacygrkvcpcFGEkvvhhdpplLFDLSRDPSETHILtpASEPVFYQVMERVQQAVWE 385
Cdd:cd16033   366 GFD------------IDE---------LYDLESDPYELNNL--IDDPEYEEILREMRTRLYE 404
Sulfatase pfam00884
Sulfatase;
63-261 4.86e-33

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 126.00  E-value: 4.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGyrvlqwtg 142
Cdd:pfam00884   1 PNVVLVLGESLRAPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTP-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 143 asGGLPTNETTFAKILKEKGYATG-------------------------------------------------------- 166
Cdd:pfam00884  73 --VGLPRTEPSLPDLLKRAGYNTGaigkwhlgwynnqspcnlgfdkffgrntgsdlyadppdvpyncsgggvsdeallde 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 167 -------------------------------------------------------------LIGRILDTLDVEGLSNSTL 185
Cdd:pfam00884 151 alefldnndkpfflvlhtlgshgppyypdrypekyatfkpsscseeqllnsydntllytddAIGRVLDKLEENGLLDNTL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217392264 186 IYFTSDHGGSLENQLGNTQYGGWNgiykggkgmGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAG 261
Cdd:pfam00884 231 VVYTSDHGESLGEGGGYLHGGKYD---------NAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
63-260 5.66e-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: 124.07  E-value: 5.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKL-TQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQwT 141
Cdd:cd00016     1 KHVVLIVLDGLGADDLGKAGNPAPTTPNLKRLASEGATFnFRSVSPPTSSAPNHAALLTGAYPTLHGYTGNGSADPEL-P 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 GASGGLPTNETTFAKILKEKGYATGL-------------------------------------------------IGRIL 172
Cdd:cd00016    80 SRAAGKDEDGPTIPELLKQAGYRTGVigllkaidetskekpfvlflhfdgpdgpghaygpntpeyydaveeiderIGKVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 173 DTLDVEGLSNSTLIYFTSDHGGSLENqLGNTqyggwngiYKGGKGMGGWEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDV 252
Cdd:cd00016   160 DALKKAGDADDTVIIVTADHGGIDKG-HGGD--------PKADGKADKSHTGMRVPFIAYGPGV-KKGGVKHELISQYDI 229

                  ....*...
gi 2217392264 253 FPTVVRLA 260
Cdd:cd00016   230 APTLADLL 237
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
63-388 4.51e-30

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: 120.83  E-value: 4.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMV------------ 130
Cdd:cd16028     1 RNVLFITADQWRADCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwngtpldarhlt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 131 ------------SSIGY---------------RVLQWTGASGGLPTN-----------ETTFA-----KILKEKG----- 162
Cdd:cd16028    81 lalelrkagydpALFGYtdtspdprglapldpRLLSYELAMPGFDPVdrldeypaedsDTAFLtdraiEYLDERQdepwf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 163 ---------------------------------------------YAT-------------------------------- 165
Cdd:cd16028   161 lhlsyirphppfvapapyhalydpadvpppiraeslaaeaaqhplLAAflerieslsfspgaanaadlddeevaqmraty 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 166 -GLI-------GRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQYGGwngiykggkGMGGWEGGIRVPGIFRWPGVL 237
Cdd:cd16028   241 lGLIaevddhlGRLFDYLKETGQWDDTLIVFTSDHG----EQLGDHWLWG---------KDGFFDQAYRVPLIVRDPRRE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 238 ---PAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLG-------TAQHSDHEFlmhycerFLHAARWHQR 307
Cdd:cd16028   308 adaTRGQVVDAFTESVDVMPTILDWLGGEIPHQ--CDGRSLLPLLAGaqpsdwrDAVHYEYDF-------RDVSTRRPQE 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 308 DRGTmwkvhfvtpvfQPEGAGACYGRkvcpcfGE--KVVHHD--PPLLFDLSRDPSETHILtpASEPVFYQVMERVQQAV 383
Cdd:cd16028   379 ALGL-----------SPDECSLAVIR------DErwKYVHFAalPPLLFDLKNDPGELRDL--AADPAYAAVVLRYAQKL 439

                  ....*
gi 2217392264 384 WEHQR 388
Cdd:cd16028   440 LSWRM 444
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-381 1.20e-29

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: 118.48  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigYRvlqwt 141
Cdd:cd16152     1 KPNVIVFFTDQQRWDTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-----FR----- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 142 gASGGLPTNETTFAKILKEKGYATGLIG---------------------------------------------------- 169
Cdd:cd16152    71 -NGIPLPADEKTLAHYFRDAGYETGYVGkwhlagyrvdaltdfaidyldnrqkdkpfflflsylephhqndrdryvapeg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 170 ----------------------------------------RILDTLDVEGLSNSTLIYFTSDHGGSLENQlgNTQYggwn 209
Cdd:cd16152   150 saerfanfwvppdlaalpgdwaeelpdylgccerldenvgRIRDALKELGLYDNTIIVFTSDHGCHFRTR--NAEY---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 210 giykggkGMGGWEGGIRVPGIFRWPGVLpAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDHE 289
Cdd:cd16152   224 -------KRSCHESSIRVPLVIYGPGFN-GGGRVEELVSLIDLPPTLLDAAGIDVPEE--MQGRSLLPLVDGKVEDWRNE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 290 FLMHYCE----RFLHAARW----HQRDRGtmWKVHFVTPVFQPEgagacygrkvcpcfgekvvhhdppLLFDLSRDPSET 361
Cdd:cd16152   294 VFIQISEsqvgRAIRTDRWkysvAAPDKD--GWKDSGSDVYVED------------------------YLYDLEADPYEL 347
                         410       420
                  ....*....|....*....|
gi 2217392264 362 HILtpASEPVFYQVMERVQQ 381
Cdd:cd16152   348 VNL--IGRPEYREVAAELRE 365
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
61-378 3.34e-29

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: 117.28  E-value: 3.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  61 SRPNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQ-HI----SAAsLCTPSRAAFLTGRYPVRSGMvssigy 135
Cdd:cd16155     1 KKPNILFILADDQRADTIGALGNPEIQTPNLDRLARRGTSFTNaYNmggwSGA-VCVPSRAMLMTGRTLFHAPE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 136 rvlqwtGASGGLPTNETTFAKILKEKGY---ATG---------------------------------------------- 166
Cdd:cd16155    74 ------GGKAAIPSDDKTWPETFKKAGYrtfATGkwhngfadaaiefleeykdgdkpffmyvaftaphdprqappeyldm 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 167 --------------------------------------------------------LIGRILDTLDVEGLSNSTLIYFTS 190
Cdd:cd16155   148 yppetiplpenflpqhpfdngegtvrdeqlapfprtpeavrqhlaeyyamithldaQIGRILDALEASGELDNTIIVFTS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 191 DHG------GSLENQlgNTQYGGWngiykggkgmggweggiRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEV 264
Cdd:cd16155   228 DHGlavgshGLMGKQ--NLYEHSM-----------------RVPLIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEI 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 265 PQDrvIDGQDLLPLLLG-TAQHSDHEFLMhycerFLHAARWHQRDRgtmWKVHFVTPvfqpegagacygrkvcpcfGEKV 343
Cdd:cd16155   288 PES--VEGKSLLPVIRGeKKAVRDTLYGA-----YRDGQRAIRDDR---WKLIIYVP-------------------GVKR 338
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2217392264 344 VhhdppLLFDLSRDPSETHILtpASEPVFYQVMER 378
Cdd:cd16155   339 T-----QLFDLKKDPDELNNL--ADEPEYQERLKK 366
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
62-275 4.46e-29

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: 114.78  E-value: 4.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLGIGDIGCYGN----------NTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM-- 129
Cdd:cd16153     1 KPNILWIITDDQRVDSLSCYNNahtgksesrlGYVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVyg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 130 -------------------------VSSIG-------YRVLQ---------WTGASGGLPTNETTFAKI---------LK 159
Cdd:cd16153    81 feaahpaldhglptfpevlkkagyqTASFGkshleafQRYLKnanqsyksfWGKIAKGADSDKPFFVRLsflqphtpvLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 160 EKGYAT------------GLIGRILDTLDVEGLSN---STLIYFTSDHGGSLENQLGNTQYGGWNgiykggkgmggweGG 224
Cdd:cd16153   161 PKEFRDrfdyyafcaygdAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQGILAKFTFWP-------------QS 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217392264 225 IRVPGIFRWPGVL--PAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVIDGQDL 275
Cdd:cd16153   228 HRVPLIVVSSDKLkaPAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDYLDGRDL 280
iduronate-2-sulfatase cd16030
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ...
61-288 8.86e-29

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: 116.90  E-value: 8.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  61 SRPNILLLMADDLGiGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGM----------- 129
Cdd:cd16030     1 KKPNVLFIAVDDLR-PWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVydnnsyfrkva 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 130 --VSSI-------GYRVL------------------QWT------------------------GASGGLPTNETTF---- 154
Cdd:cd16030    80 pdAVTLpqyfkenGYTTAgvgkifhpgipdgdddpaSWDeppnppgpekyppgklcpgkkggkGGGGGPAWEAADVpdea 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 155 ----------AKILKEKG-------------------------------------------------------------- 162
Cdd:cd16030   160 ypdgkvadeaIEQLRKLKdsdkpfflavgfykphlpfvapkkyfdlyplesiplpnpfdpidlpevawndlddlpkygdi 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 163 -----------------------------YATGLIGRILDTLDVEGLSNSTLIYFTSDHGGslenQLGntQYGGW----- 208
Cdd:cd16030   240 palnpgdpkgplpdeqarelrqayyasvsYVDAQVGRVLDALEELGLADNTIVVLWSDHGW----HLG--EHGHWgkhtl 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 209 ----NgiykggkgmggweggiRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGgeVPQDRVIDGQDLLPLLLGTAQ 284
Cdd:cd16030   314 feeaT----------------RVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAG--LPAPPCLEGKSLVPLLKNPSA 375

                  ....
gi 2217392264 285 HSDH 288
Cdd:cd16030   376 KWKD 379
sulfatase_like cd16150
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-362 7.74e-26

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: 7.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSG-------------- 128
Cdd:cd16150     1 PNIVIFVADQLRADSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGhrtlhhllrpdepn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 129 MVSSI---GYRVlQWTGASGGLPTNETTFA-------------------------------------------------- 155
Cdd:cd16150    81 LLKTLkdaGYHV-AWAGKNDDLPGEFAAEAycdsdeacvrtaidwlrnrrpdkpfclylplifphppygveepwfsmidr 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 156 --------KILKEKGYATGLI---------------------------------GRILDTLDVEGLSNSTLIYFTSDHG- 193
Cdd:cd16150   160 eklpprrpPGLRAKGKPSMLEgiekqgldrwseerwrelratylgmvsrldhqfGRLLEALKETGLYDDTAVFFFSDHGd 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 194 ------------GSLENQLgntqyggwngiykggkgmggweggIRVPGIFRWPGvLPAGRVIGEPTSLMDVFPTVVRLAG 261
Cdd:cd16150   240 ytgdyglvekwpNTFEDCL------------------------TRVPLIIKPPG-GPAGGVSDALVELVDIPPTLLDLAG 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 262 geVPQDRVIDGQDLLPLLLG-TAQHSDHEFlmhyCE-RFLHAARWHqrdrgtMWKVHFVTPVFQPEG----AGACYGRKV 335
Cdd:cd16150   295 --IPLSHTHFGRSLLPVLAGeTEEHRDAVF----SEgGRLHGEEQA------MEGGHGPYDLKWPRLlqqeEPPEHTKAV 362
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2217392264 336 cpcfgeKVVHHD---------PPLLFDLSRDPSETH 362
Cdd:cd16150   363 ------MIRTRRykyvyrlyePDELYDLEADPLELH 392
PRK13759 PRK13759
arylsulfatase; Provisional
61-369 1.02e-19

arylsulfatase; Provisional


Pssm-ID: 237491 [Multi-domain]  Cd Length: 485  Bit Score: 90.88  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  61 SRPNILLLMADDLGiGD-IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVS-------- 131
Cdd:PRK13759    5 KKPNIILIMVDQMR-GDcLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGygdvvpwn 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 132 -----------------SIG---------------------------------------YRVLQWTGASG--------GL 147
Cdd:PRK13759   84 ykntlpqefrdagyytqCIGkmhvfpqrnllgfhnvllhdgylhsgrnedksqfdfvsdYLAWLREKAPGkdpdltdiGW 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 148 -----------------PTNET---------------------TFAK--------------------------------- 156
Cdd:PRK13759  164 dcnswvarpwdleerlhPTNWVgsesieflrrrdptkpfflkmSFARphspydppkryfdmykdadipdphigdweyaed 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 157 -------------ILKEK-------GYaTGL-------IGRILDTLDVEGLSNSTLIYFTSDHGgsleNQLGNTQ----- 204
Cdd:PRK13759  244 qdpeggsidalrgNLGEEyarraraAY-YGLithidhqIGRFLQALKEFGLLDNTIILFVSDHG----DMLGDHYlfrkg 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 205 --YGGwngiykggkgmggwegGIRVPGIFRWPG---VLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLL 279
Cdd:PRK13759  319 ypYEG----------------SAHIPFIIYDPGgllAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD--VDGRSLKNLI 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 280 LG-TAQHSDHEFLMH-YCERFLHaarWHQRDRGT-MWkvHFVTPVFQpegagacygrkvcpcfgekvvhhdpplLFDLSR 356
Cdd:PRK13759  381 FGqYEGWRPYLHGEHaLGYSSDN---YLTDGKWKyIW--FSQTGEEQ---------------------------LFDLKK 428
                         490
                  ....*....|...
gi 2217392264 357 DPSETHILTPASE 369
Cdd:PRK13759  429 DPHELHNLSPSEK 441
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-294 1.90e-19

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: 88.42  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMAD------DLGIGDIGcygnntMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSI--- 133
Cdd:cd16035     1 PNILLILTDqeryppPWPAGWAA------LNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLgsp 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 134 -------------------GYRVlQW------TGASGGLPTNETTFA----KILKEKG---------------------- 162
Cdd:cd16035    75 mqpllspdvptlghmlraaGYYT-AYkgkwhlSGAAGGGYKRDPGIAaqavEWLRERGaknadgkpwflvvslvnphdim 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 163 ---------------------YATGLIGRILDTLDVEGLSNSTLIYFTSDHG------GSLENqlGNTQYGgwngiykgg 215
Cdd:cd16035   154 fppddeerwrrfrnfyynlirDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggahGLRGK--GFNAYE--------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 216 kgmggweGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDRVID----GQDLLPLLLGTAQHSDHE-F 290
Cdd:cd16035   223 -------EALHVPLIISHPDLFGTGQTTDALTSHIDLLPTLLGLAGVDAEARATEApplpGRDLSPLLTDADADAVRDgI 295

                  ....
gi 2217392264 291 LMHY 294
Cdd:cd16035   296 LFTY 299
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
63-170 4.11e-18

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: 86.28  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMvssigyrvlqWTG 142
Cdd:cd16156     1 KQFIFIMTDTQRWDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS----------WTN 70
                          90       100
                  ....*....|....*....|....*...
gi 2217392264 143 aSGGLPTNETTFAKILKEKGYATGLIGR 170
Cdd:cd16156    71 -CMALGDNVKTIGQRLSDNGIHTAYIGK 97
G6S cd16147
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ...
62-169 8.79e-15

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: 75.66  E-value: 8.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  62 RPNILLLMADDLgigDIGCYGNNTMRtPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYP----VRSGMVSSIGYRV 137
Cdd:cd16147     1 RPNIVLILTDDQ---DVELGSMDPMP-KTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgVTNNSPPGGGYPK 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217392264 138 LQWTGAsgglptNETTFAKILKEKGYATGLIG 169
Cdd:cd16147    77 FWQNGL------ERSTLPVWLQEAGYRTAYAG 102
sulfatase_like cd16154
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
63-170 2.97e-14

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: 73.54  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADDLGIGDIGCYGNNTM--RTPNIDRLAEDGVKLTqHISAASLCTPSRAAFLTGRYPVRSGmVSSIGYRVLQw 140
Cdd:cd16154     1 PNILLIIADDQGLDSSAQYSLSSDlpVTPTLDSLANSGIVFD-NLWATPACSPTRATILTGKYGFRTG-VLAVPDELLL- 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217392264 141 tgasgglpTNETTFAKILKE---KGYATGLIGR 170
Cdd:cd16154    78 --------SEETLLQLLIKDattAGYSSAVIGK 102
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
148-359 1.61e-11

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: 65.26  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 148 PTNETTFAKILKEKGY-------ATGLIGRILDTLDVEGLSNSTLIYFTSDHGgslENQLGNTQYggwngiykggKGMGG 220
Cdd:cd16171   182 PSMGENFGSIRNIRAFyyamcaeTDAMLGEIISALKDTGLLDKTYVFFTSDHG---ELAMEHRQF----------YKMSM 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 221 WEGGIRVPGIFRWPGVlPAGRVIGEPTSLMDVFPTVVRLAGGEVPQDrvIDGQDLLPLLLGTAQHSDH-----------E 289
Cdd:cd16171   249 YEGSSHVPLLIMGPGI-KAGQQVSDVVSLVDIYPTMLDIAGVPQPQN--LSGYSLLPLLSESSIKESPsrvphpdwvlsE 325
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 290 FlmHYCErfLHAARWHQRDrgTMWKvhFVTpvfqpegagacYGRkvcpcfGEKVvhhdPPLLFDLSRDPS 359
Cdd:cd16171   326 F--HGCN--VNASTYMLRT--NSWK--YIA-----------YAD------GNSV----PPQLFDLSKDPD 366
YejM COG3083
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ...
163-276 5.47e-08

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


Pssm-ID: 442317 [Multi-domain]  Cd Length: 603  Bit Score: 54.91  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 163 YATGLIGRILDTLDVEGLSNSTLIYFTSDHGGSL----ENQLG-NTQYGGWNgiykggkgmggweggIRVPGIFRWPGVL 237
Cdd:COG3083   435 YVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFnengQNYWGhNSNFSRYQ---------------LQVPLVIHWPGTP 499
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217392264 238 PagRVIGEPTSLMDVFPTVV-RLAGGEVPqdrVID---GQDLL 276
Cdd:COG3083   500 P--QVISKLTSHLDIVPTLMqRLLGVQNP---ASDysqGEDLF 537
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
168-276 2.04e-06

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 50.04  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 IGRILDTLDVEGLSNSTLIYFTSDHGGSLEnqlGNTQYggwngiykggkgmGGWEGGIRVPGIFRWPGvLPAGRVIGEPT 247
Cdd:COG1368   430 LGEFIEKLKKSGWYDNTIFVIYGDHGPRSP---GKTDY-------------ENPLERYRVPLLIYSPG-LKKPKVIDTVG 492
                          90       100
                  ....*....|....*....|....*....
gi 2217392264 248 SLMDVFPTVVRLAGGEVPQDRVIdGQDLL 276
Cdd:COG1368   493 SQIDIAPTLLDLLGIDYPSYYAF-GRDLL 520
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
44-169 9.17e-06

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 47.44  E-value: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  44 LAVLLSLAPSASSDISASRPNILLLMADDLGIGDIgcygnNTMRTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGR 122
Cdd:COG1524     5 LSLLLASLLAAAAAAAPPAKKVVLILVDGLRADLL-----ERAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217392264 123 YPVRSGMVSSIGYR--------VLQWTGASGGLPT--NETTFAKILKEKGYATGLIG 169
Cdd:COG1524    80 YPGEHGIVGNGWYDpelgrvvnSLSWVEDGFGSNSllPVPTIFERARAAGLTTAAVF 136
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
63-165 4.33e-04

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: 41.90  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264  63 PNILLLMADdlGIGD--IGCYGNNTMRTPNIDRLAEDGVKLTQHISAASLCTPSRA--AFLTGRYPVRSGMVSSIGYRvl 138
Cdd:cd16015     1 PNVIVILLE--SFSDpyIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYK-- 76
                          90       100
                  ....*....|....*....|....*..
gi 2217392264 139 qwtgasgglPTNETTFAKILKEKGYAT 165
Cdd:cd16015    77 ---------LNPLPSLPSILKEQGYET 94
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
168-261 5.87e-04

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: 41.51  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217392264 168 IGRILDTLDVEGLSNSTLIYFTSDHGGSLENQLGNTQYGGWNGIykggkgmggweggiRVPGIFRWPGVLPaGRVIGEPT 247
Cdd:cd16015   205 LGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--------------RTPLLIYSPGLKK-PKKIDRVG 269
                          90
                  ....*....|....
gi 2217392264 248 SLMDVFPTVVRLAG 261
Cdd:cd16015   270 SQIDIAPTLLDLLG 283
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
87-131 1.86e-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: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217392264  87 RTPNIDRLAEDGVKLTQHISAA-SLCTPSRAAFLTGRYPVRSGMVS 131
Cdd:pfam01663  19 LTPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVG 64
 
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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