|
Name |
Accession |
Description |
Interval |
E-value |
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
16-638 |
1.63e-157 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 467.59 E-value: 1.63e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 16 FFSLLVVLLWLKTIFaYLVDFHLGIESGIQYFI---LFINPIATTLLLLGIALY---IRRPRVAYITMMVIYFLLTLLVF 89
Cdd:COG1368 1 FFLLFLLLLSLRLVF-LLFNFDLSLGEILQAFLyglRFILYLLLLLLLLLLLLLpllFRRPKLRWIYLLLVLLLLLLLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 90 SNVTYYREFTDFITINTILGAGKVASgLGESairLFRPYDVIYWIDFIILTVLLIA----KKIKLDPRPIRARMAFAIST 165
Cdd:COG1368 80 ADILYYRFFGDRLNFSDLDYLGDTGE-VLGS---LLSSYDLLLLLDLLLLLLLLLLlyrlLKKLRKSLPWRKRLALLLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 166 LAVMIFSGNLFMaeaDRPELLSRTFSRDYLVKYLGLN-AFMVYDgvqTYQTNQVRAEASPNDMKEVENYVKEHYAAPNDd 244
Cdd:COG1368 156 LALLLLGIRLGE---DRPLNLSDAFSRNNFVNELGLNgPYSFYD---ALRNNKAPATYSEEEALEIKKYLKSNRPTPNP- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 245 lFGLAKGKNVIYIHLESFQQFLIDYKltdenGLQHEVTPFINSLYhsNSTFSFDNFFHQVkaGKTSDAETLMENSLFGLN 324
Cdd:COG1368 229 -FGPAKKPNVVVILLESFSDFFIGAL-----GNGKDVTPFLDSLA--KESLYFGNFYSQG--GRTSRGEFAVLTGLPPLP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 325 QGSlFTQLGGKNTFQAAPDILSQtQGYTSAVFHGNAGTFWNRNETYKNLGYDYFFDSSYYDVNDDNSfqYGLHDKPFFQQ 404
Cdd:COG1368 299 GGS-PYKRPGQNNFPSLPSILKK-QGYETSFFHGGDGSFWNRDSFYKNLGFDEFYDREDFDDPFDGG--WGVSDEDLFDK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 405 SVQYLERLQQPFYSKFIAVSNHYPYskfTNDEAGFPLANTNDETINGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLY 484
Cdd:COG1368 375 ALEELEKLKKPFFAFLITLSNHGPY---TLPEEDKKIPDYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 485 GDHYGVSNSRNKNLaelvgktsstwtnyDNAQMQRVPYMIHIPGQTQGGINHTYGGQVDALPTLLHLLGVDTKNYIQLGQ 564
Cdd:COG1368 452 GDHGPRSPGKTDYE--------------NPLERYRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGR 517
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488254579 565 DLFSKDHEQLVsFRDGDFVTPKYTYYGgtiysnetgeaitePTEEVQNEIDSLKEKVDKQLAVSDQINNGDLLR 638
Cdd:COG1368 518 DLLSPDTDPFA-FRNGGFITDDYVYVL--------------KTGELTEEDKELEEEALAYLQLSDYLYGNDLLR 576
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
252-553 |
4.54e-73 |
|
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: 237.97 E-value: 4.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 252 KNVIYIHLESFQQFLIDYKLTDENglqheVTPFINSLyhSNSTFSFDNFFHQVKAGKTSDAETLMENSLFGLNQGSLFTQ 331
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGED-----LTPNLNKL--AKEGLYFGNFYSPGFGGGTANGEFEVLTGLPPLPLGSGSYT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 332 LGGKNTFQAAPDILSQtQGYTSAVFHGNAGTFWNRNETYKNLGYDYFFDSSYYDVNDDNSFQYGLHDKPFFQQSVQYLER 411
Cdd:cd16015 74 LYKLNPLPSLPSILKE-QGYETIFIHGGDASFYNRDSVYPNLGFDEFYDLEDFPDDEKETNGWGVSDESLFDQALEELEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 412 LQ-QPFYSKFIAVSNHYPYSKFTNDEAGFPLANTNDETINGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHYGV 490
Cdd:cd16015 153 LKkKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488254579 491 SNSRNKNlaelvgktsstwTNYDNAQMQRVPYMIHIPGQTQGGINHTYGGQVDALPTLLHLLG 553
Cdd:cd16015 233 LGSDYDE------------TDEDPLDLYRTPLLIYSPGLKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
252-554 |
1.81e-38 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 144.49 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 252 KNVIYIHLESFQQFLIDYkltdeNGLQHEVTPFINSLyhSNSTFSFDNFFhqVKAGKTSDAETLMENSLFGLNQGSLFTQ 331
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGL-----YGYPRPTTPFLDRL--AEEGLLFSNFY--SGGTLTAPSRFALLTGLPPHNFGSYVST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 332 LGGK-NTFQAAPDILSQtQGYTSAVFHGNAGTFWNRNeTYKNLGYDYFFD----SSYYDVNDDNSFQYGLH---DKPFFQ 403
Cdd:pfam00884 72 PVGLpRTEPSLPDLLKR-AGYNTGAIGKWHLGWYNNQ-SPCNLGFDKFFGrntgSDLYADPPDVPYNCSGGgvsDEALLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 404 QSVQYLERLQQPFYSKFIAVSNHYPYSKF----TNDEAGFPLANTNDETINGYFATANYLDTAVQEFFNYLKESGLYDNS 479
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGSHGPPYYPdrypEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488254579 480 VIVLYGDHYGVSNSRNKNLaeLVGKTSSTWtnydnAQMQRVPYMIHIPGQT-QGGINHTYGGQVDALPTLLHLLGV 554
Cdd:pfam00884 230 LVVYTSDHGESLGEGGGYL--HGGKYDNAP-----EGGYRVPLLIWSPGGKaKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
252-568 |
9.30e-20 |
|
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: 89.91 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 252 KNVIYIHLESFQQfliDYklTDENGLQHEVTPFINSLyhSNSTFSFDNFFhqvkagkTSDAETLMEN-----SLFGLNQG 326
Cdd:cd16148 1 MNVILIVIDSLRA---DH--LGCYGYDRVTTPNLDRL--AAEGVVFDNHY-------SGSNPTLPSRfslftGLYPFYHG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 327 SLFTQLGGKNTFqaAPDILSQtQGYTSAVFHGNAGTFWNRnetyknlGYDyffdsSYYDVNDDNSFQYGLHDKPFFQQSV 406
Cdd:cd16148 67 VWGGPLEPDDPT--LAEILRK-AGYYTAAVSSNPHLFGGP-------GFD-----RGFDTFEDFRGQEGDPGEEGDERAE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 407 Q-------YLERLQ--QPFYSkFI-AVSNHYPYskftndeagfplantndetinGYFATANYLDTAVQEFFNYLKESGLY 476
Cdd:cd16148 132 RvtdraleWLDRNAddDPFFL-FLhYFDPHEPY---------------------LYDAEVRYVDEQIGRLLDKLKELGLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 477 DNSVIVLYGDHyGvsnsrnKNLAELvGKTSSTWTNYDNAQMqRVPYMIHIPGQTQGGINHTYGGQVDALPTLLHLLGVDT 556
Cdd:cd16148 190 EDTLVIVTSDH-G------EEFGEH-GLYWGHGSNLYDEQL-HVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEP 260
|
330
....*....|..
gi 488254579 557 KNYIQlGQDLFS 568
Cdd:cd16148 261 PDYSD-GRSLLP 271
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
342-579 |
1.43e-18 |
|
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: 87.95 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 342 PDILSQtQGYTSavfhGNAGTFWNrNETYKNLGYDYFFDSSYYDVNDDNSFQYGLHdkpFFQQSVQylerlQQPFYSkFI 421
Cdd:cd16027 84 PELLRE-AGYYT----GLIGKTHY-NPDAVFPFDDEMRGPDDGGRNAWDYASNAAD---FLNRAKK-----GQPFFL-WF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 422 AVSN-HYPYSKFTNDEAGFPLANT--------NDET---INGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHyG 489
Cdd:cd16027 149 GFHDpHRPYPPGDGEEPGYDPEKVkvppylpdTPEVredLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDH-G 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 490 VSNSRNKnlaelvgktsstWTNYDNAqmQRVPYMIHIPGQTQGG------INHtyggqVDALPTLLHLLGVDTKNYIQlG 563
Cdd:cd16027 228 MPFPRAK------------GTLYDSG--LRVPLIVRWPGKIKPGsvsdalVSF-----IDLAPTLLDLAGIEPPEYLQ-G 287
|
250
....*....|....*.
gi 488254579 564 QDLFSKDHEQLVSFRD 579
Cdd:cd16027 288 RSFLPLLKGEKDPGRD 303
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
401-590 |
1.93e-15 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 78.77 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 401 FFQQSVQYLERLQ---QPFyskFIAVS---NHYPY-------SKFTNDEAGFPLANTNDET--------INGYFATANYL 459
Cdd:COG3119 133 LTDKAIDFLERQAdkdKPF---FLYLAfnaPHAPYqapeeylDKYDGKDIPLPPNLAPRDLteeelrraRAAYAAMIEEV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 460 DTAVQEFFNYLKESGLYDNSVIVLYGDHYGVSNSRNKNLaelvGKtsstWTNYDNAqmQRVPYMIHIPGQTQ-GGINHTY 538
Cdd:COG3119 210 DDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRG----GK----GTLYEGG--IRVPLIVRWPGKIKaGSVSDAL 279
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488254579 539 GGQVDALPTLLHLLGVDTKNYIQlGQDLFSkdheqlvSFRDGDFVTPKYTYY 590
Cdd:COG3119 280 VSLIDLLPTLLDLAGVPIPEDLD-GRSLLP-------LLTGEKAEWRDYLYW 323
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
370-566 |
1.29e-13 |
|
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: 73.37 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 370 YKNLGYDYFFDSSYYDvNDDNSFQYGLHDkPFFQ--QSVQYLERL---QQPFyskFIAVS----------------NHYP 428
Cdd:cd16034 128 KGYECNHDHNNPHYYD-DDGKRIYIKGYS-PDAEtdLAIEYLENQadkDKPF---ALVLSwnpphdpyttapeeylDMYD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 429 YSKFT---NDEAGFPLANTNDETINGYFATANYLDTAVQEFFNYLKESGLYDNSVIVL---YGDHYGVSNSRNKNlaelv 502
Cdd:cd16034 203 PKKLLlrpNVPEDKKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGLLENTIVVFtsdHGDMLGSHGLMNKQ----- 277
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488254579 503 gktssTWtnYDNAqmQRVPYMIHIPGQ-TQGGINHTYGGQVDALPTLLHLLGVDTKNYIQlGQDL 566
Cdd:cd16034 278 -----VP--YEES--IRVPFIIRYPGKiKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVE-GRDL 332
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
406-552 |
1.76e-13 |
|
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: 70.53 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 406 VQYLERLQQ--PFYSKFIAVSNHYPyskfTNDEAGFPlantndetiNGYFATANYLDTAVQEFFNYLKESGLYDNSVIVL 483
Cdd:cd00016 109 LKAIDETSKekPFVLFLHFDGPDGP----GHAYGPNT---------PEYYDAVEEIDERIGKVLDALKKAGDADDTVIIV 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 484 YGDHYGVS-NSRNKNLAELVGKTSSTWTnydnaqmqRVPYMIHIPGQTQGGINHTYGGQVDALPTLLHLL 552
Cdd:cd00016 176 TADHGGIDkGHGGDPKADGKADKSHTGM--------RVPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
397-565 |
3.18e-11 |
|
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: 64.00 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 397 HDKpffqqSVQYLERLQ--QPF--YSKFIAVsnHYPYskftndeagfplantndetinGYFATANYLDTAVQEFFNYLKE 472
Cdd:cd16022 102 HDE-----AIDFIERRDkdKPFflYVSFNAP--HPPF---------------------AYYAMVSAIDDQIGRILDALEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 473 SGLYDNSVIVLYGDH---YGVSNSRNKnlaelvgKtsstWTNYDNAqmQRVPYMIHIPGQTQGG-INHTYGGQVDALPTL 548
Cdd:cd16022 154 LGLLDNTLIVFTSDHgdmLGDHGLRGK-------K----GSLYEGG--IRVPFIVRWPGKIPAGqVSDALVSLLDLLPTL 220
|
170
....*....|....*..
gi 488254579 549 LHLLGVDTKNYIQlGQD 565
Cdd:cd16022 221 LDLAGIEPPEGLD-GRS 236
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
427-566 |
5.36e-11 |
|
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: 65.29 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 427 YPYSKFTNDEAGFPLANTNDET----INGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDH-YgvsnsrnkNLAE- 500
Cdd:cd16030 234 PKYGDIPALNPGDPKGPLPDEQarelRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHgW--------HLGEh 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488254579 501 -LVGKtsstWTNYDNAqmQRVPYMIHIPGQTQGginhtyGGQVDAL-------PTLLHLLGVDTKNYIQlGQDL 566
Cdd:cd16030 306 gHWGK----HTLFEEA--TRVPLIIRAPGVTKP------GKVTDALvelvdiyPTLAELAGLPAPPCLE-GKSL 366
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
446-613 |
1.26e-08 |
|
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: 57.92 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 446 DETINGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHyGVSnsrnknLAE--LVGKtsstWTNYDNAqmQRVPYM 523
Cdd:cd16031 233 QRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDN-GFF------LGEhgLFDK----RLMYEES--IRVPLI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 524 IHIPGQTQGGInhtyggQVDAL-------PTLLHLLGVDTKNYIQlGQD---LFSKdhEQLVSFRDGDFvtpkYTYYGgt 593
Cdd:cd16031 300 IRDPRLIKAGT------VVDALvlnidfaPTILDLAGVPIPEDMQ-GRSllpLLEG--EKPVDWRKEFY----YEYYE-- 364
|
170 180
....*....|....*....|
gi 488254579 594 iysnETGEAITEPTEEVQNE 613
Cdd:cd16031 365 ----EPNFHNVPTHEGVRTE 380
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
347-566 |
4.37e-08 |
|
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: 56.01 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 347 QTQGYTSAVF---H-GNAGTFW--------NRNETYKNLGYDYFFdssYYDVNDDNSFQYGLHDKPFF---QQSVQYLER 411
Cdd:cd16144 104 KDAGYATAHFgkwHlGGEGGYGpedqgfdvNIGGTGNGGPPSYYF---PPGKPNPDLEDGPEGEYLTDrltDEAIDFIEQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 412 LQ-QPFyskFIAVSNHYPYS----------KFTNDEAGFPLANTNDEtingYFATANYLDTAVQEFFNYLKESGLYDNSV 480
Cdd:cd16144 181 NKdKPF---FLYLSHYAVHTpiqarpelieKYEKKKKGLRKGQKNPV----YAAMIESLDESVGRILDALEELGLADNTL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 481 IVLYGDHYGVSNSR-----NKNLAElvGKtsstWTNYDNAQmqRVPYMIHIPGQTQGG-INHTYGGQVDALPTLLHLLGV 554
Cdd:cd16144 254 VIFTSDNGGLSTRGgpptsNAPLRG--GK----GSLYEGGI--RVPLIVRWPGVIKPGsVSDVPVIGTDLYPTFLELAGG 325
|
250
....*....|...
gi 488254579 555 DTKNYIQL-GQDL 566
Cdd:cd16144 326 PLPPPQHLdGVSL 338
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
347-598 |
4.51e-08 |
|
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: 56.02 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 347 QTQGYTSAVFHGNAGTfwnrNETYKNLGYDYFFDSsyYDVNDDNSFQYGLHDKPFFQQSVQYLER-LQQPFyskFIAVS- 424
Cdd:cd16146 111 QDRGFDEVLGHGGGGI----GQYPDYWGNDYFDDT--YYHNGKFVKTEGYCTDVFFDEAIDFIEEnKDKPF---FAYLAt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 425 N--HYPYSKFTNDEAGFpLANTNDETINGYFATANYLDTAVQEFFNYLKESGLYDNSvIVLY----GDHYGVSNSRNknl 498
Cdd:cd16146 182 NapHGPLQVPDKYLDPY-KDMGLDDKLAAFYGMIENIDDNVGRLLAKLKELGLEENT-IVIFmsdnGPAGGVPKRFN--- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 499 AELVGKTSSTWtnyDNAQmqRVPYMIHIPGQTQGG-INHTYGGQVDALPTLLHLLGVDTKNYIQL-GQDL-------FSK 569
Cdd:cd16146 257 AGMRGKKGSVY---EGGH--RVPFFIRWPGKILAGkDVDTLTAHIDLLPTLLDLCGVKLPEGIKLdGRSLlpllkgeSDP 331
|
250 260
....*....|....*....|....*....
gi 488254579 570 DHEQLVSFRDGDFVTPKYTYYGGTIYSNE 598
Cdd:cd16146 332 WPERTLFTHSGRWPPPPKKKRNAAVRTGR 360
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
383-592 |
4.54e-08 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 55.24 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 383 YYDVNDDNSFQYglhDKPFFQQSVQYLE---RLQQPFyskFIAVSNHYPYskftndeagFPLANTND-------ETINGY 452
Cdd:cd16037 100 FRGEDQRHGFRY---DRDVTEAAVDWLReeaADDKPW---FLFVGFVAPH---------FPLIAPQEfydlyvrRARAAY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 453 FATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHyGvsnsrnKNLAE--LVGKTsstwTNYDNAqmQRVPYMIHIPGQT 530
Cdd:cd16037 165 YGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDH-G------DMLGErgLWGKS----TMYEES--VRVPMIISGPGIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 531 QGGINHTYGGQVDALPTLLHLLGVDTKNYIQlGQDLFS-----KDHEQLV------------SF--RDGDFvtpKYTYYG 591
Cdd:cd16037 232 AGKRVKTPVSLVDLAPTILEAAGAPPPPDLD-GRSLLPlaegpDDPDRVVfseyhahgspsgAFmlRKGRW---KYIYYV 307
|
.
gi 488254579 592 G 592
Cdd:cd16037 308 G 308
|
|
| PRK12363 |
PRK12363 |
phosphoglycerol transferase I; Provisional |
234-606 |
6.44e-08 |
|
phosphoglycerol transferase I; Provisional
Pssm-ID: 171438 Cd Length: 703 Bit Score: 56.07 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 234 VKEHYAAPNddlFGLAKGKNVIYIHLESFQQflidyKLTDENGLQHeVTPFINSLyhSNSTFSFDNFFHQVKAGKTSDAe 313
Cdd:PRK12363 142 VAPEYQVPQ---QPLQKRKNIVWIYGESLER-----TYFDEDVFPG-LMPNLTRL--ATEAVDVRNLASTEGSGWTIAG- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 314 tlMENSLFGLnqgSLFTQLGGKNT------FQAAPDILS---QTQGYTSAVFHGNAGTFWNRNETYKNLGYDYFFDSSYY 384
Cdd:PRK12363 210 --MVASMCGV---PLTTAQGDENSmdrmghFLPEARCLGdylKDQGYTNHYVGGADASFAGKGKFLSSHGFDEVHDVNYF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 385 DVN----DDNSFQYGLHDKPFFQ---QSVQYLERLQQPFYSKFIAVSNHYPyskftndeAG-FPLANTND--ETINGYFA 454
Cdd:PRK12363 285 LHDkgvaPKHFSAWGVHDDVLLDdayDEFETLSRAGQPFMLTTLTMDTHHP--------AGhLPSACKGQryDSPLGDIG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 455 TANYL---DTAVQEFFNYLKESGLYDNSVIVLYGDHYGVSNS--------RNKNLAELVGKTsstwtnydnaqmqrvpym 523
Cdd:PRK12363 357 MLHAIkcsDRLIGQLVDRIRNSRYGKNTIIVIASDHLAMPNDlsdvltkqKRENLLLFLGKD------------------ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 524 ihIPGQTqggINHTYGGQVDALPTLLHLLGVDTKNYiQLGQDLFSKDHEQLVSF---RDGDFVTPKYTYYGGTIYsneTG 600
Cdd:PRK12363 419 --IAPQQ---VVTRAGTTLDSGATLLQLLEPGMRTL-GFGRSLLADDAPPSASVaasRDSGKDYPRYLAFARSLW---TG 489
|
....*.
gi 488254579 601 EAITEP 606
Cdd:PRK12363 490 RSTRML 495
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
364-555 |
8.58e-08 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 53.78 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 364 WNRNETYKNLGYDYFFDSsYYDVNDDNSFQYGLHDKPFF-QQSVQYLERL---QQPFYskfiaVSNHY--PYSKFtndea 437
Cdd:cd16149 74 GSHGKTKKPEGYLEGQTT-LPEVLQDAGYRCGLSGKWHLgDDAADFLRRRaeaEKPFF-----LSVNYtaPHSPW----- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 438 gfplantndetinGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHyGVSNSRNKnlaeLVGKTSSTW-TN-YDNA 515
Cdd:cd16149 143 -------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDN-GFNMGHHG----IWGKGNGTFpLNmYDNS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488254579 516 qmQRVPYMIHIPGQTQGGI-NHTYGGQVDALPTLLHLLGVD 555
Cdd:cd16149 205 --VKVPFIIRWPGVVPAGRvVDSLVSAYDFFPTLLELAGVD 243
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
452-566 |
1.70e-07 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 54.16 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 452 YFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDH------YGvsnsrnknlaeLVGKTSSTWTNydnaQMQRVPYMIH 525
Cdd:cd16150 202 YLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHgdytgdYG-----------LVEKWPNTFED----CLTRVPLIIK 266
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488254579 526 IPGQTQGGINHTYGGQVDALPTLLHLLGVDTKnYIQLGQDL 566
Cdd:cd16150 267 PPGGPAGGVSDALVELVDIPPTLLDLAGIPLS-HTHFGRSL 306
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
397-555 |
5.39e-07 |
|
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: 52.21 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 397 HDKPFFQQSVQYLERL------QQPFyskFIAVSnhypyskFTN--DEAGFPLANTN-DETINGYFATANYLDTAVQEFF 467
Cdd:cd16035 115 RDPGIAAQAVEWLRERgaknadGKPW---FLVVS-------LVNphDIMFPPDDEERwRRFRNFYYNLIRDVDRQIGRVL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 468 NYLKESGLYDNSVIVLYGDH--YGVSNSrnknlaeLVGKTSstwTNYDnaQMQRVPYMIHIPGQ-TQGGINHTYGGQVDA 544
Cdd:cd16035 185 DALDASGLADNTIVVFTSDHgeMGGAHG-------LRGKGF---NAYE--EALHVPLIISHPDLfGTGQTTDALTSHIDL 252
|
170
....*....|.
gi 488254579 545 LPTLLHLLGVD 555
Cdd:cd16035 253 LPTLLGLAGVD 263
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
397-589 |
6.48e-07 |
|
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: 52.23 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 397 HDKPFFQqSVQYLERLQQPFYSKFIAvsNHYPYSKFTN-----DEAGFPlANTNDEtINGYFATANYLDTAVQEFFNYLK 471
Cdd:cd16152 122 KDKPFFL-FLSYLEPHHQNDRDRYVA--PEGSAERFANfwvppDLAALP-GDWAEE-LPDYLGCCERLDENVGRIRDALK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 472 ESGLYDNSVIVLYGDHYGVSNSRNKNLaelvgKTSStwtnYDNAqmQRVPYMIHIPGQTQGG-INHTYGGqVDALPTLLH 550
Cdd:cd16152 197 ELGLYDNTIIVFTSDHGCHFRTRNAEY-----KRSC----HESS--IRVPLVIYGPGFNGGGrVEELVSL-IDLPPTLLD 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488254579 551 LLGVDTKNYIQlGQDLFSKDHEQLVSFRDGDFV------------TPKYTY 589
Cdd:cd16152 265 AAGIDVPEEMQ-GRSLLPLVDGKVEDWRNEVFIqisesqvgrairTDRWKY 314
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
410-555 |
7.49e-07 |
|
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: 52.26 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 410 ERLQQPFYSKFIavsNHYPYSKFTNDEAgfPLANTNDETINGYFATanYL------DTAVQEFFNYLKESGLYDNSVIVL 483
Cdd:cd16028 199 EAAQHPLLAAFL---ERIESLSFSPGAA--NAADLDDEEVAQMRAT--YLgliaevDDHLGRLFDYLKETGQWDDTLIVF 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 484 -------YGDHYgvsnsrnknlaeLVGKtsSTWtnYDNAqmQRVPYMIHIPGQ----TQGGINHTYGGQVDALPTLLHLL 552
Cdd:cd16028 272 tsdhgeqLGDHW------------LWGK--DGF--FDQA--YRVPLIVRDPRReadaTRGQVVDAFTESVDVMPTILDWL 333
|
...
gi 488254579 553 GVD 555
Cdd:cd16028 334 GGE 336
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
378-558 |
1.97e-06 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 50.68 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 378 FFDSsyYDVND---DNSFQYGLHDKPFFQQsvQYLERLQQpfyskfiavsnhypyskFTNDEAGFplantnDETINGYFA 454
Cdd:cd16033 169 YLDM--YDPEDiplPESFADDFEDKPYIYR--RERKRWGV-----------------DTEDEEDW------KEIIAHYWG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 455 TANYLDTAVQEFFNYLKESGLYDNSVIVL---YGDHYGVSNSRNKNLAelvgktsstwtNYDnaQMQRVPYMIHIPGQTQ 531
Cdd:cd16033 222 YITLIDDAIGRILDALEELGLADDTLVIFtsdHGDALGAHRLWDKGPF-----------MYE--ETYRIPLIIKWPGVIA 288
|
170 180
....*....|....*....|....*...
gi 488254579 532 -GGINHTYGGQVDALPTLLHLLGVDTKN 558
Cdd:cd16033 289 aGQVVDEFVSLLDLAPTILDLAGVDVPP 316
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
452-566 |
1.98e-06 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 50.64 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 452 YFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDHyGVSNSRNKnlaeLVGKtsstwTNYDNAQMqRVPYMIHIPGQTQ 531
Cdd:cd16155 194 YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDH-GLAVGSHG----LMGK-----QNLYEHSM-RVPLIISGPGIPK 262
|
90 100 110
....*....|....*....|....*....|....*
gi 488254579 532 GGINHTYGGQVDALPTLLHLLGVDTKNYIQlGQDL 566
Cdd:cd16155 263 GKRRDALVYLQDVFPTLCELAGIEIPESVE-GKSL 296
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
347-587 |
2.79e-05 |
|
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: 47.05 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 347 QTQGYTSAV---FHGNAGtfwnRNETY--KNLGYDYFFDSSYY--------------DVNDDNSFQYGLHDKPFF----- 402
Cdd:cd16158 93 KTVGYQTAMvgkWHLGVG----LNGTYlpTHQGFDHYLGIPYShdqgpcqnltcfppNIPCFGGCDQGEVPCPLFynesi 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 403 -QQSVQY--LERLQQPFYSKFIA-------------VSNHYPYSKFtndeAGFPLANtndETINGYFATA-NYLDTAVQE 465
Cdd:cd16158 169 vQQPVDLltLEERYAKFAKDFIAdnakegkpfflyyASHHTHYPQF----AGQKFAG---RSSRGPFGDAlAELDGSVGE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 466 FFNYLKESGLYDNSVIVLYGDHyGVS---NSRNKNLAEL-VGKTsstwTNYDNAQmqRVPYMIHIPGQTQGGINHTYGGQ 541
Cdd:cd16158 242 LLQTLKENGIDNNTLVFFTSDN-GPStmrKSRGGNAGLLkCGKG----TTYEGGV--REPAIAYWPGRIKPGVTHELAST 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488254579 542 VDALPTLLHLLGVDTKNYIQLGQDLFSKDHEQLVSFRDGDFVTPKY 587
Cdd:cd16158 315 LDILPTIAKLAGAPLPNVTLDGVDMSPILFEQGKSPRQTFFYYPTS 360
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
342-568 |
3.12e-05 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 46.81 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 342 PDILsQTQGYTSAVF---HgnAGTFWNRNETYK--------------------NLGYDYFFDSSYYDVNDDnsfqyglhd 398
Cdd:cd16143 89 AKML-KQAGYRTAMVgkwH--LGLDWKKKDGKKaatgtgkdvdyskpikggplDHGFDYYFGIPASEVLPT--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 399 kpFFQQSVQYLERL---QQPFYSKFIAVSNHYPYskftndeagfplanTNDETINGYfATAN-Y------LDTAVQEFFN 468
Cdd:cd16143 157 --LTDKAVEFIDQHakkDKPFFLYFALPAPHTPI--------------VPSPEFQGK-SGAGpYgdfvyeLDWVVGRILD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 469 YLKESGLYDNSVIVLYGDHyGVSNSRNKNLAELVGKTSS------TWTNYDNAqmQRVPYMIHIPGQT-QGGINHTYGGQ 541
Cdd:cd16143 220 ALKELGLAENTLVIFTSDN-GPSPYADYKELEKFGHDPSgplrgmKADIYEGG--HRVPFIVRWPGKIpAGSVSDQLVSL 296
|
250 260
....*....|....*....|....*..
gi 488254579 542 VDALPTLLHLLGVDTKNyiQLGQDLFS 568
Cdd:cd16143 297 TDLFATLAAIVGQKLPD--NAAEDSFS 321
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
356-555 |
2.62e-04 |
|
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.
Pssm-ID: 293753 [Multi-domain] Cd Length: 393 Bit Score: 44.08 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 356 FHGNAGTFWNRNETYKNLGYDYFFDSSYYDVNDDNSfQYGLH---------------DKPFF----QQSV----QYLERL 412
Cdd:cd16029 125 YYGGAEDYYTHTSGGANDYGNDDLRDNEEPAWDYNG-TYSTDlftdravdiienhdpSKPLFlylaFQAVhaplQVPPEY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 413 QQPFYSKFiavSNHYPYSKFTndeagfplantndetingYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGD----HY 488
Cdd:cd16029 204 ADPYEDKF---AHIKDEDRRT------------------YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDnggpTG 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488254579 489 GVSNSRNknlAELVGKTSSTW---TnydnaqmqRVPYMIHIP------GQTQGGINHTyggqVDALPTLLHLLGVD 555
Cdd:cd16029 263 GGDGGSN---YPLRGGKNTLWeggV--------RVPAFVWSPllppkrGTVSDGLMHV----TDWLPTLLSLAGGD 323
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
350-555 |
2.83e-04 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 43.74 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 350 GYTSavfHGNAGTF-----WnRNETYKNLGYDYFFDSSYYDVNDDNSFQYGlHDKpFFQQSVQYLERLQ-QPFY------ 417
Cdd:cd16145 124 GYLD---QVHAHNYypeylW-RNGEKVPLPNNVIPPLDEGNNAGGGGGTYS-HDL-FTDEALDFIRENKdKPFFlylayt 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 418 ---SKFIAVSNHYPYSKFTNDEAGFPLANTNDETinGYFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGD----HYGV 490
Cdd:cd16145 198 lphAPLQVPDDGPYKYKPKDPGIYAYLPWPQPEK--AYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDngphSEGG 275
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 491 SNSRNKNL---AELVG-KTSstwtNYDNAqmQRVPYMIHIPGQTQ-GGINHTYGGQVDALPTLLHLLGVD 555
Cdd:cd16145 276 SEHDPDFFdsnGPLRGyKRS----LYEGG--IRVPFIARWPGKIPaGSVSDHPSAFWDFMPTLADLAGAE 339
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
386-553 |
3.64e-04 |
|
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: 43.57 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 386 VNDDNSFQYGLHDKPFFqqsvqylerlqqpFYSKFiavsNHYPYSKFTNDEagfpLANTNDETIngYFATANYLDTAVQE 465
Cdd:cd16160 181 VGDAKSFIEDNQENPFF-------------LYFSF----PQTHTPLFASKR----FKGKSKRGR--YGDNINEMSWAVGE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 466 FFNYLKESGLYDNSVIVLYGDH--------YGVSNSRNKNlaelvGKTSStwtnYDNAQmqRVPYMIHIPGQTQGGINHT 537
Cdd:cd16160 238 VLDTLVDTGLDQNTLVFFLSDHgphveyclEGGSTGGLKG-----GKGNS----WEGGI--RVPFIAYWPGTIKPRVSHE 306
|
170
....*....|....*.
gi 488254579 538 YGGQVDALPTLLHLLG 553
Cdd:cd16160 307 VVSTMDIFPTFVDLAG 322
|
|
| 7tm_1 |
pfam00001 |
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ... |
17-171 |
3.76e-03 |
|
7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.
Pssm-ID: 459624 [Multi-domain] Cd Length: 256 Bit Score: 39.59 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 17 FSLLVVLLWLkTIFAYLVDFHLGiESG--IQYFILFINPIATTLLLLGIAL--Y-----------IRRPRVAYITMMVIY 81
Cdd:pfam00001 33 FSLLTLPFWL-VYYLNHGDWPFG-SALckIVGALFVVNGYASILLLTAISIdrYlaivhplrykrRRTPRRAKVLILVIW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 82 FL-----LTLLVFSNVTYYREFTD---FITINTILGAgKVASGLGESAIRLFRPYDVI---YWidFIILTVLLIAKKIKL 150
Cdd:pfam00001 111 VLalllsLPPLLFGWTLTVPEGNVtvcFIDFPEDLSK-PVSYTLLISVLGFLLPLLVIlvcYT--LIIRTLRKSASKQKS 187
|
170 180
....*....|....*....|.
gi 488254579 151 DPRPIRARMAFAISTLAVMIF 171
Cdd:pfam00001 188 SERTQRRRKALKTLAVVVVVF 208
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
452-487 |
4.97e-03 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 39.43 E-value: 4.97e-03
10 20 30
....*....|....*....|....*....|....*.
gi 488254579 452 YFATANYLDTAVQEFFNYLKESGLYDNSVIVLYGDH 487
Cdd:cd16021 178 YLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDH 213
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
457-554 |
9.74e-03 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 38.73 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488254579 457 NYLDTAVQEFFNYLKESGLYDNSVIVLYGD---HYGVSNSRNKNLAELV-GKTSSTWTnydnaqmqRVPYMIHIPGQTQG 532
Cdd:cd16151 212 AYMDKLVGKLVDKLEELGLRENTIIIFTGDngtHRPITSRTNGREVRGGkGKTTDAGT--------HVPLIVNWPGLIPA 283
|
90 100
....*....|....*....|....*
gi 488254579 533 GinHTYGGQVDA---LPTLLHLLGV 554
Cdd:cd16151 284 G--GVSDDLVDFsdfLPTLAELAGA 306
|
|
| |
