|
Name |
Accession |
Description |
Interval |
E-value |
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-532 |
0e+00 |
|
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: 604.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTSLT 234
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWATPACSPTRATILTGKYGFRTGVLAVPDELLLSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 235 TLPRFLAENDASKAYSMAVFGKWHLGGGDPDLSHPNsaGVGHYVGNITGTLDDYSDWTLTDNGSQTQVTQYHTSKVTDLA 314
Cdd:cd16154 81 TLLQLLIKDATTAGYSSAVIGKWHLGGNDNSPNNPG--GIPYYAGILGGGVQDYYNWNLTNNGQTTNSTEYATTKLTNLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 315 MDWITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGSAeDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDERENTLV 394
Cdd:cd16154 159 IDWIDQQTKPWFLWLAYNAPHTPFHLPPAELHSRSLLGDSA-DIEANPRPYYLAAIEAMDTEIGRLLASIDEEERENTII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 395 IFIGDNGTPAPVIDTSvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSF 474
Cdd:cd16154 238 IFIGDNGTPGQVVDLP-YTRNHAKGSLYEGGINVPLIVSGAGVERANERESALVNATDLYATIAELAGVDAAEIHDSVSF 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 475 YDTLFDVvpNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQ 532
Cdd:cd16154 317 KPLLSDV--NASTRQYNYTEYESPTTTGWATRNQYYKLIESENGQEELYDLINDPSEQ 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
150-551 |
2.46e-83 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 265.20 E-value: 2.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 150 PPVSKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFV--- 225
Cdd:COG3119 19 AAAKRPNILFILADDLGYGDLG--CYGNPLIKTPNIDRLAAEGVRFTNAYVTsPVCSPSRASLLTGRYPHRTGVTDNgeg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 -PAVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLgggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtq 304
Cdd:COG3119 97 yNGGLPPDEPTLAELLKEAG----YRTALFGKWHL--------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 305 YHTSKVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPPN----------ELHTRSELSGSAEDIAQNPRPYYLAAIE 371
Cdd:COG3119 128 YLTDLLTDKAIDFLERQADkdkPFFLYLAFNAPHAPYQAPEEyldkydgkdiPLPPNLAPRDLTEEELRRARAAYAAMIE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 372 AMDTEIGRLLASLptDE---RENTLVIFIGDNGTPAPVidtsvYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLV 448
Cdd:COG3119 208 EVDDQVGRLLDAL--EElglADNTIVVFTSDNGPSLGE-----HGLRGGKGTLYEGGIRVPLIVRWPGKIKAGSVSDALV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 449 NSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQRNGvAGWAVRNQDYKLL--SIDSQQQALFDMN 526
Cdd:COG3119 281 SLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTG--EKAEWRDYLYWEYPRGG-GNRAIRTGRWKLIryYDDDGPWELYDLK 357
|
410 420
....*....|....*....|....*
gi 1482818008 527 VDINEQNDLlqsGDDWSALVLELAE 551
Cdd:COG3119 358 NDPGETNNL---AADYPEVVAELRA 379
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
155-535 |
3.10e-68 |
|
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: 226.28 E-value: 3.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDasnqysystDL-----P--KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPA 227
Cdd:cd16146 1 PNVILILTDDQGYG---------DLgfhgnPilKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTGVWHTIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 V---MDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDPdlSHPNSAG----VGHYVGNITGTLD----DYSDWTLTDN 296
Cdd:cd16146 72 GrerMRLDETTLAEVFKDA----GYRTGIFGKWHLGDNYP--YRPQDRGfdevLGHGGGGIGQYPDywgnDYFDDTYYHN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 297 GSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLPPnelhtrsELSGSAEDIAQNP-RPYYLAAIEAMD 374
Cdd:cd16146 146 GKFVKTEGYCTDVFFDEAIDFIeENKDKPFFAYLATNAPHGPLQVPD-------KYLDPYKDMGLDDkLAAFYGMIENID 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASL-PTDERENTLVIFIGDNGTPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDL 453
Cdd:cd16146 219 DNVGRLLAKLkELGLEENTIVIFMSDNGPAGGVPKRFNAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVDTLTAHIDL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 454 YATIVQIAGGDITQV--YNSHSFYDTLFDVVPNPSVRQYNYADFQRNGV----AGWAVRNQDYKLLSIDSQQQALFDMNV 527
Cdd:cd16146 299 LPTLLDLCGVKLPEGikLDGRSLLPLLKGESDPWPERTLFTHSGRWPPPpkkkRNAAVRTGRWRLVSPKGFQPELYDIEN 378
|
....*...
gi 1482818008 528 DINEQNDL 535
Cdd:cd16146 379 DPGEENDV 386
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
155-538 |
9.48e-65 |
|
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: 217.41 E-value: 9.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV---- 228
Cdd:cd16144 1 PNIVLILVDDLGWaDLG---CYGSKFYETPNIDRLAKEGMRFTQAYAAaPVCSPSRASILTGQYPARLGITDVIPGrrgp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 --------------MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPdlSHPNSAGvghYVGNITGT------LDDY 288
Cdd:cd16144 78 pdntklipppsttrLPLEEVTIAEALKDAG----YATAHFGKWHLGGEGG--YGPEDQG---FDVNIGGTgnggppSYYF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 289 SDWTLTDNGSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHlPPNELHTRSELSGSAEDIAQNpRPYYL 367
Cdd:cd16144 149 PPGKPNPDLEDGPEGEYLTDRLTDEAIDFIeQNKDKPFFLYLSHYAVHTPIQ-ARPELIEKYEKKKKGLRKGQK-NPVYA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 368 AAIEAMDTEIGRLLASLptDE---RENTLVIFIGDNG--TPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNT 442
Cdd:cd16144 227 AMIESLDESVGRILDAL--EElglADNTLVIFTSDNGglSTRGGPPTSNAPLRGGKGSLYEGGIRVPLIVRWPGVIKPGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 443 RESRLVNSTDLYATIVQIAGGDITQVYN--SHSFYDTLFDVVPNPSVR-----QYNYADfQRNGVAGwAVRNQDYKLL-S 514
Cdd:cd16144 305 VSDVPVIGTDLYPTFLELAGGPLPPPQHldGVSLVPLLKGGEADLPRRalfwhFPHYHG-QGGRPAS-AIRKGDWKLIeF 382
|
410 420
....*....|....*....|....
gi 1482818008 515 IDSQQQALFDMNVDINEQNDLLQS 538
Cdd:cd16144 383 YEDGRVELYNLKNDIGETNNLAAE 406
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
155-535 |
3.42e-62 |
|
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: 208.90 E-value: 3.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASnqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGV---SFVPAVMD 230
Cdd:cd16027 1 PNILWIIADDLSPDLG---GYGGNVVKTPNLDRLAAEGVRFTNAFTTaPVCSPSRSALLTGLYPHQNGAhglRSRGFPLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHPNSAGVGHYVGNITGTLDDYSDWTLTDNGSQtqvtqyhtskv 310
Cdd:cd16027 78 DGVKTLPELLREAG----YYTGLIGKTHYNPDAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRAKKGQ----------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 311 tdlamdwitqqtsPWFVWLAYVAPHSPFHLPPNE--LHTRSELS---------GSAEDIAQnprpyYLAAIEAMDTEIGR 379
Cdd:cd16027 143 -------------PFFLWFGFHDPHRPYPPGDGEepGYDPEKVKvppylpdtpEVREDLAD-----YYDEIERLDQQVGE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 380 LLASLPTD-ERENTLVIFIGDNGTPAPvidtsvyarqHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIV 458
Cdd:cd16027 205 ILDELEEDgLLDNTIVIFTSDHGMPFP----------RAKGTLYDSGLRVPLIVRWPGKIKPGSVSDALVSFIDLAPTLL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 459 QIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQRNGVAGW---AVRNQDYKLL-SIDSQQqaLFDMNVDINEQND 534
Cdd:cd16027 275 DLAGIEPPEYLQGRSFLPLLKG--EKDPGRDYVFAERDRHDETYDpirSVRTGRYKYIrNYMPEE--LYDLKNDPDELNN 350
|
.
gi 1482818008 535 L 535
Cdd:cd16027 351 L 351
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-535 |
3.58e-59 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 201.29 E-value: 3.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQY---SYstdlpKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFvpAVMDT 231
Cdd:cd16151 1 PNIILIMADDLGYECIGCYggeSY-----KTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNFRNYVVF--GYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAEndasKAYSMAVFGKWHLGGGDPDLSHPNSAGvghyvgnitgtLDDYSDWTLTD---------------- 295
Cdd:cd16151 74 KQKTFGHLLKD----AGYATAIAGKWQLGGGRGDGDYPHEFG-----------FDEYCLWQLTEtgekysrpatptfnir 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVT--QYHTSKVTDLAMDWITQQTS-PWFVWLAYVAPHSPF-HLPPNELHTRSElsgsaEDIAQNPRpYYLAAIE 371
Cdd:cd16151 139 NGKLLETTegDYGPDLFADFLIDFIERNKDqPFFAYYPMVLVHDPFvPTPDSPDWDPDD-----KRKKDDPE-YFPDMVA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 372 AMDTEIGRLLASLptDE---RENTLVIFIGDNGTPAPVidTSVY---ARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRES 445
Cdd:cd16151 213 YMDKLVGKLVDKL--EElglRENTIIIFTGDNGTHRPI--TSRTngrEVRGGKGKTTDAGTHVPLIVNWPGLIPAGGVSD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 446 RLVNSTDLYATIVQIAGGDITQVYNS--HSFYDTLFDVVPNPSVRQY--NYADFQRNGVAGWaVRNQDYKLLSIDSqqqa 521
Cdd:cd16151 289 DLVDFSDFLPTLAELAGAPLPEDYPLdgRSFAPQLLGKTGSPRREWIywYYRNPHKKFGSRF-VRTKRYKLYADGR---- 363
|
410
....*....|....
gi 1482818008 522 LFDMNVDINEQNDL 535
Cdd:cd16151 364 FFDLREDPLEKNPL 377
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
155-535 |
6.19e-56 |
|
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: 193.15 E-value: 6.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVdasNQYSY-STDLPKTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSF------VPA 227
Cdd:cd16029 1 PHIVFILADDLGW---NDVGFhGSDQIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHgvilagEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDPDLSHPN----------SAGVGHYVGNITGTLDDYSDWTLTDNG 297
Cdd:cd16029 78 GLPLNETLLPQYLKEL----GYATHLVGKWHLGFYTWEYTPTNrgfdsfygyyGGAEDYYTHTSGGANDYGNDDLRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 S-QTQVTQYHTSKVTDLAMDWITQ--QTSPWFVWLAYVAPHSPFHLPPNELhtrSELSGSAEDIAQNPRPYYLAAIEAMD 374
Cdd:cd16029 154 PaWDYNGTYSTDLFTDRAVDIIENhdPSKPLFLYLAFQAVHAPLQVPPEYA---DPYEDKFAHIKDEDRRTYAAMVSALD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASLptDER---ENTLVIFIGDNGTPAPVIDT-SVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESR-LVN 449
Cdd:cd16029 231 ESVGNVVDAL--KAKgmlDNTLIVFTSDNGGPTGGGDGgSNYPLRGGKNTLWEGGVRVPAFVWSPLLPPKRGTVSDgLMH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 450 STDLYATIVQIAGGDITQVYN--SHSFYDTLFDvvPNPSVRQ---YNYaDFQRNGVAGWAVRNQDYKLLSIDSqqqaLFD 524
Cdd:cd16029 309 VTDWLPTLLSLAGGDPDDLPPldGVDQWDALSG--GAPSPRTeilLNI-DDITRTTGGAAIRVGDWKLIVGKP----LFN 381
|
410
....*....|.
gi 1482818008 525 MNVDINEQNDL 535
Cdd:cd16029 382 IENDPCERNDL 392
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
155-465 |
9.89e-55 |
|
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: 184.95 E-value: 9.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTDlpKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFV---PAVMD 230
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNPDI--KTPNLDRLAAEGVRFTNAYVAsPVCSPSRASLLTGRYPHRHGVRGNvgnGGGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWHlgggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqyhtskv 310
Cdd:cd16022 79 PDEPTLAELLKEAG----YRTALIGKWH---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 311 tDLAMDWITQQ--TSPWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLASL-PTD 387
Cdd:cd16022 103 -DEAIDFIERRdkDKPFFLYVSFNAPHPPFA--------------------------YYAMVSAIDDQIGRILDALeELG 155
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1482818008 388 ERENTLVIFIGDNGTPapvidTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDI 465
Cdd:cd16022 156 LLDNTLIVFTSDHGDM-----LGDHGLRGKKGSLYEGGIRVPFIVRWPGKIPAGQVSDALVSLLDLLPTLLDLAGIEP 228
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
154-535 |
8.19e-51 |
|
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: 179.30 E-value: 8.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDdqgvdasnQYSYST-----DLP-KTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVP 226
Cdd:cd16034 1 KPNILFIFAD--------QHRAQAlgcagDDPvKTPNLDRLAKEGVVFTNAVSNyPVCSPYRASLLTGQYPLTNGVFGND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 227 AVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHPNSA--------GVGHYVGNitGTLDDYSD---WTltD 295
Cdd:cd16034 73 VPLPPDAPTIADVLKDAG----YRTGYIGKWHLDGPERNDGRADDYtppperrhGFDYWKGY--ECNHDHNNphyYD--D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVTQYHTSKVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHL---------PPNELHTRSELSGSAEDIAQNPR 363
Cdd:cd16034 145 DGKRIYIKGYSPDAETDLAIEYLENQADkdkPFALVLSWNPPHDPYTTapeeyldmyDPKKLLLRPNVPEDKKEEAGLRE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 364 --PYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNGTpapvidtsvyarQH------SKNSLYEGGIRVPLLVSG 434
Cdd:cd16034 225 dlRGYYAMITALDDNIGRLLDALKeLGLLENTIVVFTSDHGD------------MLgshglmNKQVPYEESIRVPFIIRY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 435 NLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPNPSVRQYNY------ADFQRNGVAGWAVRNQ 508
Cdd:cd16034 293 PGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQcfvpfgGGSARDGGEWRGVRTD 372
|
410 420
....*....|....*....|....*..
gi 1482818008 509 DYKLLSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16034 373 RYTYVRDKNGPWLLFDNEKDPYQLNNL 399
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
155-535 |
3.14e-50 |
|
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: 177.78 E-value: 3.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTD-LPKTPILDSLATSGVVFDNAWATPA-CTTTRGTIMTGMH----GVNSGV--SFV 225
Cdd:cd16143 1 PNIVIILADDLGYgDIS---CYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSvCTPSRYGLLTGRYpwrsRLKGGVlgGFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 PAVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLShpnsagvGHYVGNITGTLDDYSDWTL---TDNG----- 297
Cdd:cd16143 78 PPLIEPDRVTLAKMLKQAG----YRTAMVGKWHLGLDWKKKD-------GKKAATGTGKDVDYSKPIKggpLDHGfdyyf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 --SQTQVTQYHTSKvtdlAMDWITQQ---TSPWFVWLAYVAPHSPfHLPPNELHTRSELSGsaediaqnprpyYLAAIEA 372
Cdd:cd16143 147 giPASEVLPTLTDK----AVEFIDQHakkDKPFFLYFALPAPHTP-IVPSPEFQGKSGAGP------------YGDFVYE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 373 MDTEIGRLLASL-PTDERENTLVIFIGDNGTPAPVIDTSVYARQH--------SKNSLYEGGIRVPLLVSGNLLNKQNTR 443
Cdd:cd16143 210 LDWVVGRILDALkELGLAENTLVIFTSDNGPSPYADYKELEKFGHdpsgplrgMKADIYEGGHRVPFIVRWPGKIPAGSV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 444 ESRLVNSTDLYATIVQIAGGDI--TQVYNSHSFYDTLFDvVPNPSVRQYNyadFQRNGVAGWAVRNQDYKLL-------- 513
Cdd:cd16143 290 SDQLVSLTDLFATLAAIVGQKLpdNAAEDSFSFLPALLG-PKKQEVRESL---VHHSGNGSFAIRKGDWKLIdgtgsggf 365
|
410 420
....*....|....*....|....*....
gi 1482818008 514 SIDSQQQA-------LFDMNVDINEQNDL 535
Cdd:cd16143 366 SYPRGKEKlglppgqLYNLSTDPGESNNL 394
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
153-535 |
7.34e-49 |
|
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: 175.02 E-value: 7.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDA-SnqySYSTDLPKTPILDSLATSGVVFDNAWATPA-CTTTRGTIMTGM----HGVNsgvSFVP 226
Cdd:cd16031 1 KRPNIIFILTDDHRYDAlG---CYGNPIVKTPNIDRLAKEGVRFDNAFVTTSiCAPSRASILTGQyshrHGVT---DNNG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 227 AVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGGGDpdlSHPNsAGVGHYV---GNItgtldDYSDWTLTDNGSQTQVT 303
Cdd:cd16031 75 PLFDASQPTYPKLLRKA----GYQTAFIGKWHLGSGG---DLPP-PGFDYWVsfpGQG-----SYYDPEFIENGKRVGQK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 304 QYHTSKVTDLAMDWI--TQQTSPWFVWLAYVAPHSPF-------------HLPPNELHTRSELSGSAEdIAQNPRPY--- 365
Cdd:cd16031 142 GYVTDIITDKALDFLkeRDKDKPFCLSLSFKAPHRPFtpaprhrglyedvTIPEPETFDDDDYAGRPE-WAREQRNRirg 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 366 ------------------YLAAIEAMDTEIGRLLASLptDER---ENTLVIFIGDNGtpapvidtsVYARQH---SKNSL 421
Cdd:cd16031 221 vldgrfdtpekyqrymkdYLRTVTGVDDNVGRILDYL--EEQglaDNTIIIYTSDNG---------FFLGEHglfDKRLM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 422 YEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQ----YNYADFQR 497
Cdd:cd16031 290 YEESIRVPLIIRDPRLIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLLEG--EKPVDWRkefyYEYYEEPN 367
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1482818008 498 -NGVAGW-AVRNQDYKLLSIDSQQQA--LFDMNVDINEQNDL 535
Cdd:cd16031 368 fHNVPTHeGVRTERYKYIYYYGVWDEeeLYDLKKDPLELNNL 409
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
155-535 |
7.21e-48 |
|
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: 172.01 E-value: 7.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGMHGVNSGV-SFVPAVMDT 231
Cdd:cd16145 1 PNIIFILADDLGYgDLG---CYGQKKIKTPNLDRLAAEGMRFTQHYAgAPVCAPSRASLLTGLHTGHTRVrGNSEPGGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENDASKAYSMAVFGKWHLGGGDPDlSHPNSAGVGHYVGNIT---------------GTLDDY----SDWT 292
Cdd:cd16145 78 PLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTP-GHPTKQGFDYFYGYLDqvhahnyypeylwrnGEKVPLpnnvIPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 293 LTDNGSQTQVTQYHTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLP---PNELHTRSELSGSAEDIAQnPRPYYLA 368
Cdd:cd16145 157 DEGNNAGGGGGTYSHDLFTDEALDFIrENKDKPFFLYLAYTLPHAPLQVPddgPYKYKPKDPGIYAYLPWPQ-PEKAYAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 369 AIEAMDTEIGRLLASLptDE---RENTLVIFIGDNG-------TPAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLN 438
Cdd:cd16145 236 MVTRLDRDVGRILALL--KElgiDENTLVVFTSDNGphseggsEHDPDFFDSNGPLRGYKRSLYEGGIRVPFIARWPGKI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 439 KQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvVPNPSVRQYNYADFQRNGvAGWAVRNQDYKLLSIDSQ 518
Cdd:cd16145 314 PAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLG-KPQQQQHDYLYWEFYEGG-GAQAVRMGGWKAVRHGKK 391
|
410
....*....|....*....
gi 1482818008 519 QQA--LFDMNVDINEQNDL 535
Cdd:cd16145 392 DGPfeLYDLSTDPGETNNL 410
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
154-535 |
6.22e-47 |
|
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: 169.16 E-value: 6.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdasnqysYStDLP------KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGM--HGVNSGVsfv 225
Cdd:cd16025 2 RPNILLILADDLG--------FS-DLGcfggeiPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRnhHQVGMGT--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 pavMDTSLT--------------TLPRFLAENDaskaYSMAVFGKWHLGGGDpdlshpnsagvghyvgnitgtlddysdw 291
Cdd:cd16025 70 ---MAELATgkpgyegylpdsaaTIAEVLKDAG----YHTYMSGKWHLGPDD---------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 292 tltdngsqtqvtqYHTSKV-TDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPP------------------NELHTR- 348
Cdd:cd16025 115 -------------YYSTDDlTDKAIEYIDEQKApdkPFFLYLAFGAPHAPLQAPKewidkykgkydagwdalrEERLERq 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 349 ---------SELSGSAEDIA------QNPRPY-------YLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNG---- 401
Cdd:cd16025 182 kelglipadTKLTPRPPGVPawdslsPEEKKLearrmevYAAMVEHMDQQIGRLIDYLKeLGELDNTLIIFLSDNGasae 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 402 --------TPapvidtsvyARQHsKNSLYEGGIRVPLLVSG-NLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSH 472
Cdd:cd16025 262 pgwanasnTP---------FRLY-KQASHEGGIRTPLIVSWpKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGV 331
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1482818008 473 --------SFYDTLFD-VVPNPSVRQYnyadFQRNGvaGWAVRNQDYKLLSI-----DSQQQALFDMNVDINEQNDL 535
Cdd:cd16025 332 pqlpldgvSLLPTLDGaAAPSRRRTQY----FELFG--NRAIRKGGWKAVALhpppgWGDQWELYDLAKDPSETHDL 402
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
155-462 |
1.04e-45 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 162.98 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYStdLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV-MDTS 232
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYP--RPTTPFLDRLAEEGLLFSNFYSGgTLTAPSRFALLTGLPPHNFGSYVSTPVgLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LTTLPRFLAEndasKAYSMAVFGKWHLGGGDPDlsHPNSAGVGHYVGNITGtLDDYSDWTltDNGSQTQVTQYHTSKVTD 312
Cdd:pfam00884 79 EPSLPDLLKR----AGYNTGAIGKWHLGWYNNQ--SPCNLGFDKFFGRNTG-SDLYADPP--DVPYNCSGGGVSDEALLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 313 LAMDWITQQTSPWFVWLAYVAPHSPFHLPpNELHTRSELSGSAEDIAQNPRPYYLAAIEAMDTEIGRLLASLPTDE-REN 391
Cdd:pfam00884 150 EALEFLDNNDKPFFLVLHTLGSHGPPYYP-DRYPEKYATFKPSSCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGlLDN 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:pfam00884 229 TLVVYTSDHG--ESLGEGGGYLHGGKYDNAPEGGYRVPLLIWSPGGKAKGQKSEALVSHVDLFPTILDLAG 297
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
154-535 |
4.96e-45 |
|
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: 163.89 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdasnqY----SYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAV 228
Cdd:cd16026 1 KPNIVVILADDLG------YgdlgCYGSPLIKTPNIDRLAAEGVRFTDFYAAaPVCSPSRAALLTGRYPVRVGLPGVVGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 ------MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPdlSHPNSAGVGHYVG---------NITGTLDDYSDW-- 291
Cdd:cd16026 75 pgskggLPPDEITIAEVLKKAG----YRTALVGKWHLGHQPE--FLPTRHGFDEYFGipysndmwpFPLYRNDPPGPLpp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 292 ------TLTDNGSQTQVTQYHTSKvtdlAMDWITQQT-SPWFVWLAYVAPHSPfhlppneLHTRSELSGSAEDIAqnprp 364
Cdd:cd16026 149 lmeneeVIEQPADQSSLTQRYTDE----AVDFIERNKdQPFFLYLAHTMPHVP-------LFASEKFKGRSGAGL----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 365 yYLAAIEAMDTEIGRLLASLptDE---RENTLVIFIGDNGtpaPVIDTSVYA-----RQHSKNSLYEGGIRVPLLVSGNL 436
Cdd:cd16026 213 -YGDVVEELDWSVGRILDAL--KElglEENTLVIFTSDNG---PWLEYGGHGgsagpLRGGKGTTWEGGVRVPFIAWWPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 437 LNKQNTRESRLVNSTDLYATIVQIAGGDITQ--VYNSHSFYDTLFDVvpNPSVRQ---YNYADFQRNgvagwAVRNQDYK 511
Cdd:cd16026 287 VIPAGTVSDELASTMDLLPTLAALAGAPLPEdrVIDGKDISPLLLGG--SKSPPHpffYYYDGGDLQ-----AVRSGRWK 359
|
410 420 430
....*....|....*....|....*....|....*....
gi 1482818008 512 LL-------------SIDSQQQA--LFDMNVDINEQNDL 535
Cdd:cd16026 360 LHlpttyrtgtdpggLDPTKLEPplLYDLEEDPGETYNV 398
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
153-535 |
1.60e-41 |
|
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: 153.49 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDASNQYSySTDLpKTPILDSLATSGVVFDNA-----WATPACTTTRGTIMTGMHGVNSGVSfVPA 227
Cdd:cd16155 1 KKPNILFILADDQRADTIGALG-NPEI-QTPNLDRLARRGTSFTNAynmggWSGAVCVPSRAMLMTGRTLFHAPEG-GKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAY-SMAVfGKWHLGggdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqyh 306
Cdd:cd16155 78 AIPSDDKTWPETFKKA----GYrTFAT-GKWHNG---------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 307 tskVTDLAMDWITQQTS---PWFVWLAYVAPHSP------FH---------LPPN----------ELHTRSEL----SGS 354
Cdd:cd16155 107 ---FADAAIEFLEEYKDgdkPFFMYVAFTAPHDPrqappeYLdmyppetipLPENflpqhpfdngEGTVRDEQlapfPRT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 355 AEDIAQNPRPYYlAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvyAR-QHS---KNSLYEGGIRVP 429
Cdd:cd16155 184 PEAVRQHLAEYY-AMITHLDAQIGRILDALeASGELDNTIIVFTSDHGL----------AVgSHGlmgKQNLYEHSMRVP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 430 LLVSGNLLnKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQY---NYADFQRngvagwAVR 506
Cdd:cd16155 253 LIISGPGI-PKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRG--EKKAVRDTlygAYRDGQR------AIR 323
|
410 420 430
....*....|....*....|....*....|...
gi 1482818008 507 NQDYKLL----SIDSQQqaLFDMNVDINEQNDL 535
Cdd:cd16155 324 DDRWKLIiyvpGVKRTQ--LFDLKKDPDELNNL 354
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
153-535 |
5.84e-38 |
|
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: 145.02 E-value: 5.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDD--------QGVDAsnqysystdlpKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVS 223
Cdd:cd16030 1 KKPNVLFIAVDDlrpwlgcyGGHPA-----------KTPNIDRLAARGVLFTNAYCQqPVCGPSRASLLTGRRPDTTGVY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 224 FVPAVMDTSL---TTLPRFLAENDaskaYSMAVFGK-WHlGGGDPDLSHPNS--------------AGVGHYVGNITGTL 285
Cdd:cd16030 70 DNNSYFRKVApdaVTLPQYFKENG----YTTAGVGKiFH-PGIPDGDDDPASwdeppnppgpekypPGKLCPGKKGGKGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 286 DDYSDWTLTDNGSqtqvTQYHTSKVTDLAMDWITQ---QTSPWFVWLAYVAPHSPFH----------------------- 339
Cdd:cd16030 145 GGGPAWEAADVPD----EAYPDGKVADEAIEQLRKlkdSDKPFFLAVGFYKPHLPFVapkkyfdlyplesiplpnpfdpi 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 340 -LPPNELHTRSELSGSAEDIAQNPRPY---------------YLAAIEAMDTEIGRLLASLptDE---RENTLVIFIGDN 400
Cdd:cd16030 221 dLPEVAWNDLDDLPKYGDIPALNPGDPkgplpdeqarelrqaYYASVSYVDAQVGRVLDAL--EElglADNTIVVLWSDH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 401 GtpapvidtsvyarQH-------SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHS 473
Cdd:cd16030 299 G-------------WHlgehghwGKHTLFEEATRVPLIIRAPGVTKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKS 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1482818008 474 FYDTLFDvvPNPSVRQYNYADFQRNGVAGWAVRNQDYKL----LSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16030 366 LVPLLKN--PSAKWKDAAFSQYPRPSIMGYSIRTERYRYtewvDFDKVGAEELYDHKNDPNEWKNL 429
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-537 |
9.60e-36 |
|
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: 138.51 E-value: 9.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGM----HGVNSGVSFVPAV- 228
Cdd:cd16033 1 PNILFIMTDQQRYDTLG--CYGNPIVKTPNIDRLAAEGVRFTNAYTpSPVCCPARASLLTGLypheHGVLNNVENAGAYs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 --MDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHpnsagvgHYvgnitgtlDDYSDwtltdngsqtqVTQYH 306
Cdd:cd16033 79 rgLPPGVETFSEDLREAG----YRNGYVGKWHVGPEETPLDY-------GF--------DEYLP-----------VETTI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 307 TSKVTDLAMDWI---TQQTSPWFVWLAYVAPHSPFHLP-------------------------P----NELHTRSELSGS 354
Cdd:cd16033 129 EYFLADRAIEMLeelAADDKPFFLRVNFWGPHDPYIPPepyldmydpediplpesfaddfedkPyiyrRERKRWGVDTED 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 355 AEDIAQNPRpYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNGtpapviDTSVYARQHSK-NSLYEGGIRVPLLV 432
Cdd:cd16033 209 EEDWKEIIA-HYWGYITLIDDAIGRILDALEeLGLADDTLVIFTSDHG------DALGAHRLWDKgPFMYEETYRIPLII 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 SGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPnPSVRQYNYADFQRNGVAGW--AVRNQDY 510
Cdd:cd16033 282 KWPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLLRGEQP-EDWRDEVVTEYNGHEFYLPqrMVRTDRY 360
|
410 420
....*....|....*....|....*..
gi 1482818008 511 KLLSIDSQQQALFDMNVDINEQNDLLQ 537
Cdd:cd16033 361 KYVFNGFDIDELYDLESDPYELNNLID 387
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
155-464 |
2.48e-35 |
|
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: 136.51 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVdaSNQYSYSTDLP---KTPILDSLATSGVVFDNAWATPACTTTRGTIMTGMHGVNSGVSFVPavMDT 231
Cdd:cd16142 1 PNILVILGDDIGW--GDLGCYGGGIGrgaPTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGLTTVG--LPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SL-------TTLPRFLAENDaskaYSMAVFGKWHLggGDPDLSHPNSAGVGHYVGNITGTLDDYsdwtltdngsqtqvtq 304
Cdd:cd16142 77 SPgglppwePTLAELLKDAG----YATAQFGKWHL--GDEDGRLPTDHGFDEFYGNLYHTIDEE---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 305 yhtskVTDLAMDWITQQTS---PWFVWLAYVAPHSPFHLPPnelhtrsELSGSAEDIAQnprpyYLAAIEAMDTEIGRLL 381
Cdd:cd16142 135 -----IVDKAIDFIKRNAKadkPFFLYVNFTKMHFPTLPSP-------EFEGKSSGKGK-----YADSMVELDDHVGQIL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 382 ASLptDE---RENTLVIFIGDNG-----------TPapvidtsvyaRQHSKNSLYEGGIRVPLLVS--GNLlnKQNTRES 445
Cdd:cd16142 198 DAL--DElgiADNTIVIFTTDNGpeqdvwpdggyTP----------FRGEKGTTWEGGVRVPAIVRwpGKI--KPGRVSN 263
|
330
....*....|....*....
gi 1482818008 446 RLVNSTDLYATIVQIAGGD 464
Cdd:cd16142 264 EIVSHLDWFPTLAALAGAP 282
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-528 |
3.06e-35 |
|
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: 134.98 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVSFVPAVMDTSL 233
Cdd:cd16037 1 PNILIIMSDEHNPDAMG--CYGHPVVRTPNLDRLAARGTRFENAYTPsPICVPSRASFLTGRYVHETGVWDNADPYDGDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 234 TTLPRFLAEndasKAYSMAVFGKWHLGGGDPDlshpnsaGVGHYvgnitgtlDDYsdwtltdngsqtqvtqyhtskVTDL 313
Cdd:cd16037 79 PSWGHALRA----AGYETVLIGKLHFRGEDQR-------HGFRY--------DRD---------------------VTEA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 314 AMDWIT---QQTSPWFVWLAYVAPHSPFHLPPN--ELHTRSELSGsaediaqnprpyYLAAIEAMDTEIGRLLASL-PTD 387
Cdd:cd16037 119 AVDWLReeaADDKPWFLFVGFVAPHFPLIAPQEfyDLYVRRARAA------------YYGLVEFLDENIGRVLDALeELG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 388 ERENTLVIFIGDNGtpapviDTSVYARQHSKNSLYEGGIRVPLLVSGNlLNKQNTRESRLVNSTDLYATIVQIAGGDITQ 467
Cdd:cd16037 187 LLDNTLIIYTSDHG------DMLGERGLWGKSTMYEESVRVPMIISGP-GIPAGKRVKTPVSLVDLAPTILEAAGAPPPP 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482818008 468 VYNSHSFYDTLFDvvPNPSVR----QYNYADfqrNGVAGWAVRNQDYKLLSIDSQQQALFDMNVD 528
Cdd:cd16037 260 DLDGRSLLPLAEG--PDDPDRvvfsEYHAHG---SPSGAFMLRKGRWKYIYYVGYPPQLFDLEND 319
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
154-532 |
3.97e-35 |
|
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: 136.06 E-value: 3.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGV-DASNQYSYSTDlpKTPILDSLATSGVVFDNaW--ATPACTTTRGTIMTGMHGVNSGVSFVPAVmd 230
Cdd:cd16161 1 KPNFLLLFADDLGWgDLGANWAPNAI--LTPNLDKLAAEGTRFVD-WysAASVCSPSRASLMTGRLGLRNGVGHNFLP-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLP---RFLAENDASKAYSMAVFGKWHLggGDPDLSHPNSAGVGHYVGnitgtlDDYSDwtltdngsQTQVTQYHT 307
Cdd:cd16161 76 TSVGGLPlneTTLAEVLRQAGYATGMIGKWHL--GQREAYLPNSRGFDYYFG------IPFSH--------DSSLADRYA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 308 SKVTDLAMDwITQQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSGsaediaqnprpyYLAAIEAMDTEIGRLLASLPTD 387
Cdd:cd16161 140 QFATDFIQR-ASAKDRPFFLYAALAHVHVPLANLPRFQSPTSGRGP------------YGDALQEMDDLVGQIMDAVKHA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 388 E-RENTLVIFIGDNGTP------APVIDTSVYARQH----SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYAT 456
Cdd:cd16161 207 GlKDNTLTWFTSDNGPWevkcelAVGPGTGDWQGNLggsvAKASTWEGGHREPAIVYWPGRIPANSTSAALVSTLDIFPT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 457 IVQIAGGDI--TQVYNSHSFYDTLFDVVPNPSVRQYNYADFQRNGVAGWAVRNQDYKLLSIDSQQQA------------- 521
Cdd:cd16161 287 VVALAGASLppGRIYDGKDLSPVLFGGSKTGHRCLFHPNSGAAGAGALSAVRCGDYKAHYATGGALAccgstgpklyhdp 366
|
410
....*....|...
gi 1482818008 522 --LFDMNVDINEQ 532
Cdd:cd16161 367 plLFDLEVDPAES 379
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-474 |
8.34e-35 |
|
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: 132.29 E-value: 8.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYstDLPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVsfVPAVMDTSL 233
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGY--DRVTTPNLDRLAAEGVVFDNHYSGsNPTLPSRFSLFTGLYPFYHGV--WGGPLEPDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 234 TTLPRFLAENDaskaYSMAVFGkwhlgggdpdlSHPNSAGVGHYVGNItgtldDYSDWTLTDNGSQTQVTQYHTSKVTDL 313
Cdd:cd16148 77 PTLAEILRKAG----YYTAAVS-----------SNPHLFGGPGFDRGF-----DTFEDFRGQEGDPGEEGDERAERVTDR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 314 AMDWITQQTS--PWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLASLP-TDERE 390
Cdd:cd16148 137 ALEWLDRNADddPFFLFLHYFDPHEPYL--------------------------YDAEVRYVDEQIGRLLDKLKeLGLLE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 391 NTLVIF-------IGDNGtpapvidtsVYARQHSknSLYEGGIRVPLLVSGnLLNKQNTRESRLVNSTDLYATIVQIAGG 463
Cdd:cd16148 191 DTLVIVtsdhgeeFGEHG---------LYWGHGS--NLYDEQLHVPLIIRW-PGKEPGKRVDALVSHIDIAPTLLDLLGV 258
|
330
....*....|.
gi 1482818008 464 DITQVYNSHSF 474
Cdd:cd16148 259 EPPDYSDGRSL 269
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-464 |
1.37e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 125.81 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDAsnQYSYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTG----MHGV-------NSGV 222
Cdd:cd16149 1 PNILFILTDDQGPWA--LGCYGNSEAVTPNLDRLAAEGVRFENFFcTSPVCSPARASLLTGrmpsQHGIhdwivegSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 223 SFVPAVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLGggdpdlshpnsagvghyvgnitgtlDDYSDWTLTDNGSQTqv 302
Cdd:cd16149 79 TKKPEGYLEGQTTLPEVLQDA----GYRCGLSGKWHLG-------------------------DDAADFLRRRAEAEK-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 303 tqyhtskvtdlamdwitqqtsPWFVWLAYVAPHSPFHlppnelhtrselsgsaediaqnprpyYLAAIEAMDTEIGRLLA 382
Cdd:cd16149 128 ---------------------PFFLSVNYTAPHSPWG--------------------------YFAAVTGVDRNVGRLLD 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 383 SLPT-DERENTLVIFIGDNGtpapvidtsVYARQH---------SKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTD 452
Cdd:cd16149 161 ELEElGLTENTLVIFTSDNG---------FNMGHHgiwgkgngtFPLNMYDNSVKVPFIIRWPGVVPAGRVVDSLVSAYD 231
|
330
....*....|..
gi 1482818008 453 LYATIVQIAGGD 464
Cdd:cd16149 232 FFPTLLELAGVD 243
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
153-555 |
6.73e-31 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 125.94 E-value: 6.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 153 SKPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSG-VSFVPAVMD 230
Cdd:PRK13759 5 KKPNIILIMVDQMRGDCLG--CNGNKAVETPNLDMLASEGYNFENAYsAVPSCTPARAALLTGLSQWHHGrVGYGDVVPW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 231 TSLTTLPRFLAENDaskaYSMAVFGKWH------LGGGDPDLSHPNSAGVGH-YVGNITGTLDDYSDW----------TL 293
Cdd:PRK13759 83 NYKNTLPQEFRDAG----YYTQCIGKMHvfpqrnLLGFHNVLLHDGYLHSGRnEDKSQFDFVSDYLAWlrekapgkdpDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 294 TDNG--SQTQVT-------QYH-TSKVTDLAMDWIT--QQTSPWFVWLAYVAPHSPFHlPPN------------------ 343
Cdd:PRK13759 159 TDIGwdCNSWVArpwdleeRLHpTNWVGSESIEFLRrrDPTKPFFLKMSFARPHSPYD-PPKryfdmykdadipdphigd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 344 -ELHTRSELSGSA---------EDIAQNPRPYYLAAIEAMDTEIGRLLASLPT-DERENTLVIFIGDNGtpapvidtSVY 412
Cdd:PRK13759 238 wEYAEDQDPEGGSidalrgnlgEEYARRARAAYYGLITHIDHQIGRFLQALKEfGLLDNTIILFVSDHG--------DML 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 413 ARQH--SKNSLYEGGIRVPLLVS--GNLLNKQNTRES-RLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSV 487
Cdd:PRK13759 310 GDHYlfRKGYPYEGSAHIPFIIYdpGGLLAGNRGTVIdQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNLIFG--QYEGW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 488 RQY-------NYADFQrngvagWAVRNQD-YKLLSIDSQQQaLFDMNVDINEQNDLLQSG------DDW-SALVLELAEY 552
Cdd:PRK13759 388 RPYlhgehalGYSSDN------YLTDGKWkYIWFSQTGEEQ-LFDLKKDPHELHNLSPSEkyqprlREMrKKLVDHLRGR 460
|
...
gi 1482818008 553 GQS 555
Cdd:PRK13759 461 EEG 463
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
154-465 |
9.49e-31 |
|
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: 123.81 E-value: 9.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDaSNQYSYstdLPKTPILdsLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGV---------- 222
Cdd:cd16147 1 RPNIVLILTDDQDVE-LGSMDP---MPKTKKL--LADQGTTFTNAFVTtPLCCPSRASILTGQYAHNHGVtnnsppgggy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 223 -SFVPAVMDTslTTLPRFLaendaSKA-YSMAVFGKwHLGG-GDPDLSHPNSAGVGHYVGNITGTLDDYsdWTLTDNGSQ 299
Cdd:cd16147 75 pKFWQNGLER--STLPVWL-----QEAgYRTAYAGK-YLNGyGVPGGVSYVPPGWDEWDGLVGNSTYYN--YTLSNGGNG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 300 TQV----TQYHTSKVTDLAMDWIT---QQTSPWFVWLAYVAPHSPFHLPPNELHTRSELSG----SAEDIAQNPRPYYLA 368
Cdd:cd16147 145 KHGvsypGDYLTDVIANKALDFLRraaADDKPFFLVVAPPAPHGPFTPAPRYANLFPNVTApprpPPNNPDVSDKPHWLR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 369 A--------IEAMDTE--------------IGRLLASL-PTDERENTLVIFIGDNGtpapvidtsvY-----ARQHSKNS 420
Cdd:cd16147 225 RlpplnptqIAYIDELyrkrlrtlqsvddlVERLVNTLeATGQLDNTYIIYTSDNG----------YhlgqhRLPPGKRT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1482818008 421 LYEGGIRVPLLVSG-NLlnKQNTRESRLVNSTDLYATIVQIAGGDI 465
Cdd:cd16147 295 PYEEDIRVPLLVRGpGI--PAGVTVDQLVSNIDLAPTILDLAGAPP 338
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
154-484 |
1.13e-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: 120.41 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGVsFVPAV-MDT 231
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLG--CYGQPLDLTPNLDALAEEGVLFENAFtPQPVCGPARACLQTGLYPTETGC-FRNGIpLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENDaskaYSMAVFGKWHLGGgdpdlshpnsagvghyvgnitgtlddysdwtltdngsqtqvtqYHTSKVT 311
Cdd:cd16152 78 DEKTLAHYFRDAG----YETGYVGKWHLAG-------------------------------------------YRVDALT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 312 DLAMDWIT--QQTSPWFVWLAYVAPHspfHlpPNELHTRSELSGSAE---------DIA------QNPRPYYLAAIEAMD 374
Cdd:cd16152 111 DFAIDYLDnrQKDKPFFLFLSYLEPH---H--QNDRDRYVAPEGSAErfanfwvppDLAalpgdwAEELPDYLGCCERLD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 375 TEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvyarqH-------SKNSLYEGGIRVPLLVSGNLLNKqNTRESR 446
Cdd:cd16152 186 ENVGRIRDALkELGLYDNTIIVFTSDHGC-------------HfrtrnaeYKRSCHESSIRVPLVIYGPGFNG-GGRVEE 251
|
330 340 350
....*....|....*....|....*....|....*...
gi 1482818008 447 LVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDVVPN 484
Cdd:cd16152 252 LVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLVDGKVED 289
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
154-467 |
1.46e-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: 117.86 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDA----SNQYSYSTDLP----KTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGV-S 223
Cdd:cd16153 1 KPNILWIITDDQRVDSlscyNNAHTGKSESRlgyvESPNIDALAAEGVLFTNAYcNSPVCVPSRTSMLTGRYPHRTGVyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 224 FVPA--VMDTSLTTLPRFLAENdaskAYSMAVFGKWHLgggdpdlshpnsagvghyvgnitgtlDDYSDWTltDNGSQTQ 301
Cdd:cd16153 81 FEAAhpALDHGLPTFPEVLKKA----GYQTASFGKSHL--------------------------EAFQRYL--KNANQSY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 302 VTQYHTSKvtdlamdWITQQTSPWFVWLAYVAPHSPFhLPPNELhtRSelsgsaediaqnpRPYYLAAIEAMDTEIGRLL 381
Cdd:cd16153 129 KSFWGKIA-------KGADSDKPFFVRLSFLQPHTPV-LPPKEF--RD-------------RFDYYAFCAYGDAQVGRAV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 382 -----ASLPTDeRENTLVIFIGDNGtpAPVIDTSVYArqhsKNSLYEGGIRVPLLV--SGNLLNKQNTRESRLVNSTDLY 454
Cdd:cd16153 186 eafkaYSLKQD-RDYTIVYVTGDHG--WHLGEQGILA----KFTFWPQSHRVPLIVvsSDKLKAPAGKVRHDFVEFVDLA 258
|
330
....*....|...
gi 1482818008 455 ATIVQIAGGDITQ 467
Cdd:cd16153 259 PTLLAAAGVDVDA 271
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
155-536 |
4.03e-29 |
|
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: 120.56 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTdlPKTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHG-VNSGVSFVPAVMDTS 232
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGNKA--MKTPNLDRLAAEGVRFDSAYTTqPVCGPARSGLFTGLYPhTNGSWTNCMALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LtTLPRFLAENDASKAYsmavFGKWHLGGGD-------PDLSHPNsagvghYVGNITGTLDDYSD-----W-----TLTD 295
Cdd:cd16156 79 K-TIGQRLSDNGIHTAY----IGKWHLDGGDyfgngicPQGWDPD------YWYDMRNYLDELTEeerrkSrrgltSLEA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQTQVTQYHtsKVTDLAMDWITQ-QTSPWFVWLAYVAPHSPFHLPP-----------------------NELHTR--- 348
Cdd:cd16156 148 EGIKEEFTYGH--RCTNRALDFIEKhKDEDFFLVVSYDEPHHPFLCPKpyasmykdfefpkgenayddlenKPLHQRlwa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 349 -SELSGSAEDIAQNPrPYYLAAIEAMDTEIGRLLASLPtDERENTLVIFIGDNGtpapvidTSVYARQ-HSKN-SLYEGG 425
Cdd:cd16156 226 gAKPHEDGDKGTIKH-PLYFGCNSFVDYEIGRVLDAAD-EIAEDAWVIYTSDHG-------DMLGAHKlWAKGpAVYDEI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 426 IRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYADFQR-----NGV 500
Cdd:cd16156 297 TNIPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATIED--PEIPENRGVFVEFGRyevdhDGF 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1482818008 501 AGW----AVRNQDYK----LLSIDSqqqaLFDMNVDINEQNDLL 536
Cdd:cd16156 375 GGFqpvrCVVDGRYKlvinLLSTDE----LYDLEKDPYEMHNLI 414
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
155-551 |
1.92e-28 |
|
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: 118.13 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGMHGVNSGV--SFVPavMDT 231
Cdd:cd16028 1 RNVLFITADQWRADCLS--CLGHPLVKTPNLDRLAAEGVRFRNHYTqAAPCGPSRASLYTGRYLMNHRSvwNGTP--LDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENdaskAYSMAVFGKWHLGGgDPDLSHPNSAGVGHYVGNITG-----TLDDY----SDwtltdngsqtqv 302
Cdd:cd16028 77 RHLTLALELRKA----GYDPALFGYTDTSP-DPRGLAPLDPRLLSYELAMPGfdpvdRLDEYpaedSD------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 303 tqyhTSKVTDLAMDWI-TQQTSPWFVWLAYVAPHSPFHLP-P-NELHTRSELS------GSAEDIAQNP----------- 362
Cdd:cd16028 140 ----TAFLTDRAIEYLdERQDEPWFLHLSYIRPHPPFVAPaPyHALYDPADVPppiraeSLAAEAAQHPllaafleries 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 363 ---------------------RPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvYARQH---S 417
Cdd:cd16028 216 lsfspgaanaadlddeevaqmRATYLGLIAEVDDHLGRLFDYLkETGQWDDTLIVFTSDHGE---------QLGDHwlwG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 418 KNSLYEGGIRVPLLV---SGNLLNKQNTRESRLVNSTDLYATIVQIAGGDITQVYNSHS-----------------FYDT 477
Cdd:cd16028 287 KDGFFDQAYRVPLIVrdpRREADATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGRSllpllagaqpsdwrdavHYEY 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1482818008 478 LFDVVPNPSVRQynYADFQRNGVAGWAVRNQDYKLLSIDSQQQALFDMNVDINEQNDLlqSGD-DWSALVLELAE 551
Cdd:cd16028 367 DFRDVSTRRPQE--ALGLSPDECSLAVIRDERWKYVHFAALPPLLFDLKNDPGELRDL--AADpAYAAVVLRYAQ 437
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
155-464 |
9.73e-25 |
|
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: 104.97 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNqySYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMH----GVNSGVSFVPAvm 229
Cdd:cd16032 1 PNILLIMADQLTAAALP--AYGNTVVKTPNLDRLAARGVVFDNAYcNSPLCAPSRASMMTGRLpsriGAYDNAAEFPA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 230 dtSLTTLPRFLAendaSKAYSMAVFGKWHLGGgdPDLSHpnsagvGHyvgnitgtldDYSDwtltdngsqtQVTQYHTSK 309
Cdd:cd16032 77 --DIPTFAHYLR----AAGYRTALSGKMHFVG--PDQLH------GF----------DYDE----------EVAFKAVQK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 310 VTDLAMDwitQQTSPWFVWLAYVAPHSPFHLPPN--ELHTRselsgsaediaqNPRPYYLAAIEAMDTEIGRLLASLP-T 386
Cdd:cd16032 123 LYDLARG---EDGRPFFLTVSFTHPHDPYVIPQEywDLYVR------------RARRAYYGMVSYVDDKVGQLLDTLErT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 387 DERENTLVIFIGDNGtpapviDT-----SVYarqhsKNSLYEGGIRVPLLVSGNLLnKQNTRESRLVNSTDLYATIVQIA 461
Cdd:cd16032 188 GLADDTIVIFTSDHG------DMlgergLWY-----KMSFFEGSARVPLIISAPGR-FAPRRVAEPVSLVDLLPTLVDLA 255
|
...
gi 1482818008 462 GGD 464
Cdd:cd16032 256 GGG 258
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
154-485 |
2.12e-24 |
|
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: 105.97 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNQYSYSTDLPkTPIlDSLATSGVVFDNAWATPA-CTTTRGTIMTGMHGVNSGV-----SFVPa 227
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQER-GPI-DDMAAEGIRFTQAYSADSvCTPSRAALLTGRLPIRSGMyggtrVFLP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 vmdTSLTTLPRF---LAENDASKAYSMAVFGKWHLGGGD---PDLSH-PNSAG---VGHYV--GNI-----TGTLDDYSD 290
Cdd:cd16160 78 ---WDIGGLPKTevtMAEALKEAGYTTGMVGKWHLGINEnnhSDGAHlPSHHGfdfVGTNLpfTNSwacddTGRHVDFPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 291 WT---LTDNGSQTQVTQYHTSKVTDLAMDWI----TQQTSPWFVWLAYVAPHSPfhlppneLHTRSELSGSAEdiaqnpR 363
Cdd:cd16160 155 RSacfLYYNDTIVEQPIQHEHLTETLVGDAKsfieDNQENPFFLYFSFPQTHTP-------LFASKRFKGKSK------R 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 364 PYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGtPAPVI-----DTSVYarQHSKNSLYEGGIRVPLLV--SGN 435
Cdd:cd16160 222 GRYGDNINEMSWAVGEVLDTLvDTGLDQNTLVFFLSDHG-PHVEYcleggSTGGL--KGGKGNSWEGGIRVPFIAywPGT 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1482818008 436 LlnkQNTRESRLVNSTDLYATIVQIAGGDI--TQVYNSHSFYDTLFDVVPNP 485
Cdd:cd16160 299 I---KPRVSHEVVSTMDIFPTFVDLAGGTLptDRIYDGLSITDLLLGEADSP 347
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
154-545 |
4.01e-22 |
|
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: 99.44 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGVDASNQYSYSTDLpkTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTGMHGVNSGVsfVPAVMD-T 231
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYGHPSSS--TPNLDRLAANGLRFTDFYSSsPVCSPSRAALLTGRYQVRSGV--YPGVFYpG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPR---FLAENDASKAYSMAVFGKWHLGGGDPDLSHPNSAGVGHYVG-----------NITGTLDDYSDWTLTDNG 297
Cdd:cd16158 77 SRGGLPLnetTIAEVLKTVGYQTAMVGKWHLGVGLNGTYLPTHQGFDHYLGipyshdqgpcqNLTCFPPNIPCFGGCDQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 298 SQTQVTQYHTSKV-------------TDLAMDWIT---QQTSPWFVWLAYVAPHSPfhlppnelhtrsELSGsAEDIAQN 361
Cdd:cd16158 157 EVPCPLFYNESIVqqpvdlltleeryAKFAKDFIAdnaKEGKPFFLYYASHHTHYP------------QFAG-QKFAGRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 362 PRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapviDTSVYARQHS-------KNSLYEGGIRVPLLV- 432
Cdd:cd16158 224 SRGPFGDALAELDGSVGELLQTLkENGIDNNTLVFFTSDNGP-----STMRKSRGGNagllkcgKGTTYEGGVREPAIAy 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 -SGNLlnkQNTRESRLVNSTDLYATIVQIAGGDITQV-----------YNSH-SFYDTLFDVVPNPS-------VRQYNY 492
Cdd:cd16158 299 wPGRI---KPGVTHELASTLDILPTIAKLAGAPLPNVtldgvdmspilFEQGkSPRQTFFYYPTSPDpdkgvfaVRWGKY 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1482818008 493 -ADFQRNGVAGWAVRN-QDYKLLSIDSQQQA--LFDMNVDINEQNDLLQSGDDWSAL 545
Cdd:cd16158 376 kAHFYTQGAAHSGTTPdKDCHPSAELTSHDPplLFDLSQDPSENYNLLGLPEYNQVL 432
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
154-465 |
1.98e-20 |
|
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: 94.66 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGV-DASnqySYSTDLPKTPILDSLATSGV-VFDNAWATPACTTTRGTIMTGMHGVNSG-VSF------ 224
Cdd:cd16159 1 KPNIVLFMADDLGIgDVG---CFGNDTIRTPNIDRLAKEGVkLTHHLAAAPLCTPSRAAFLTGRYPIRSGmASShgmrvi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 225 ----VPAVMDTSLTTLPRFLAENdaskAYSMAVFGKWHLG-----GGDpDLSHPNSAGVGHYVGNITGTLDDYSDwtlTD 295
Cdd:cd16159 78 lftaSSGGLPPNETTFAEVLKQQ----GYSTALIGKWHLGlhcesRND-FCHHPLNHGFDYFYGLPLTNLKDCGD---GS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 NGSQT--------QVTQYHTSKVTDLAMDWITQQTS----------------PWFVWLAYVAP----------------- 334
Cdd:cd16159 150 NGEYDlsfdplfpLLTAFVLITALTIFLLLYLGAVSkrffvfllilsllfisLFFLLLITNRYfncilmrnhevveqpms 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 335 --------------------HSPFHLPPNELHTRSELSGSAEDIAQNPRPYYLAAIEAMDTEIGRLLASLptDE---REN 391
Cdd:cd16159 230 lenltqrltkeaisflernkERPFLLVMSFLHVHTALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDAL--DElglKDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLY---------EGGIRVPLLVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:cd16159 308 TFVYFTSDNG--GHLEEISVGGEYGGGNGGIyggkkmggwEGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAG 385
|
...
gi 1482818008 463 GDI 465
Cdd:cd16159 386 APL 388
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-468 |
6.37e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 90.73 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqgvdasnQYSYSTDLPKT------PILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMH----GV--NSG 221
Cdd:cd16035 1 PNILLILTD--------QERYPPPWPAGwaalnlPARERLAANGLSFENHYtAACMCSPSRSTLYTGLHpqqtGVtdTLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 222 VSFVPaVMDTSLTTLPRFLAENDaskaYSMAVFGKWHLGGGDPDLSHpnsagvghyvgnitgtlddysdwtltdngsqtq 301
Cdd:cd16035 73 SPMQP-LLSPDVPTLGHMLRAAG----YYTAYKGKWHLSGAAGGGYK--------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 302 vtqyHTSKVTDLAMDWITQQTS------PWFVWLAYVAPHSpFHLPPNElhtrselsgsaEDIAQNPRPYYLAAIEAMDT 375
Cdd:cd16035 115 ----RDPGIAAQAVEWLRERGAknadgkPWFLVVSLVNPHD-IMFPPDD-----------EERWRRFRNFYYNLIRDVDR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 376 EIGRLLASL-PTDERENTLVIFIGDNGTPApvidtSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTRESRLVNSTDLY 454
Cdd:cd16035 179 QIGRVLDALdASGLADNTIVVFTSDHGEMG-----GAHGLRGKGFNAYEEALHVPLIISHPDLFGTGQTTDALTSHIDLL 253
|
330
....*....|....
gi 1482818008 455 ATIVQIAGGDITQV 468
Cdd:cd16035 254 PTLLGLAGVDAEAR 267
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
155-473 |
3.48e-18 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 86.44 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWA-TPACTTTRGTIMTGM--HGVNSGVSFvpAVMDT 231
Cdd:cd16171 1 PNVVMVMSD--SFDGRLTFRPGNQVVDLPYINFMKQHGSVFLNAYTnSPICCPSRAAMWSGLftHLTESWNNY--KGLDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 232 SLTTLPRFLAENdaskAYSMAVFGKWHLGGGDpdlsHPNSAGVGHYVGNITGTLDDYSDWT--LTDNGSQTQVtQYHTSK 309
Cdd:cd16171 77 NYPTWMDRLEKH----GYHTQKYGKLDYTSGH----HSVSNRVEAWTRDVPFLLRQEGRPTvnLVGDRSTVRV-MLKDWQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 310 VTDLAMDWITQ----QTSPWFVWLAYVAPHsPFHLPpnelhTRSELSGSAEDIaqnpRPYYLAAIEAMDTEIGRLLASL- 384
Cdd:cd16171 148 NTDKAVHWIRKeapnLTQPFALYLGLNLPH-PYPSP-----SMGENFGSIRNI----RAFYYAMCAETDAMLGEIISALk 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 385 PTDERENTLVIFIGDNGtpapviDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNtRESRLVNSTDLYATIVQIAGGD 464
Cdd:cd16171 218 DTGLLDKTYVFFTSDHG------ELAMEHRQFYKMSMYEGSSHVPLLIMGPGIKAGQ-QVSDVVSLVDIYPTMLDIAGVP 290
|
....*....
gi 1482818008 465 ITQVYNSHS 473
Cdd:cd16171 291 QPQNLSGYS 299
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
154-462 |
1.14e-16 |
|
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: 82.51 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 154 KPNIILIISDDQGvdASNQYSYSTDLPKTPILDSLATSGVVFDNAW-ATPACTTTRGTIMTGMHGVNSGVSFVPAVMDTS 232
Cdd:cd16157 1 KPNIILMLMDDMG--WGDLGVFGEPSRETPNLDRMAAEGMLFTDFYsANPLCSPSRAALLTGRLPIRNGFYTTNAHARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 LT-------------TLPRFLAENdaskAYSMAVFGKWHLG----------GGDPDLSHPNsAGVGHYVGNITGTLDDYS 289
Cdd:cd16157 79 YTpqnivggipdseiLLPELLKKA----GYRNKIVGKWHLGhrpqyhplkhGFDEWFGAPN-CHFGPYDNKAYPNIPVYR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 290 DWTLTD----------NGSQTQVTQYHTSKvtdlAMDWITQQTS---PWFVWLAYVAPHSPFHLPPNELHTRSelsgsae 356
Cdd:cd16157 154 DWEMIGryyeefkidkKTGESNLTQIYLQE----ALEFIEKQHDaqkPFFLYWAPDATHAPVYASKPFLGTSQ------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 357 diaqnpRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGtpAPVIDTSVYARQHS-----KNSLYEGGIRVPL 430
Cdd:cd16157 223 ------RGLYGDAVMELDSSVGKILESLkSLGIENNTFVFFSSDNG--AALISAPEQGGSNGpflcgKQTTFEGGMREPA 294
|
330 340 350
....*....|....*....|....*....|..
gi 1482818008 431 LVSGNLLNKQNTRESRLVNSTDLYATIVQIAG 462
Cdd:cd16157 295 IAWWPGHIKPGQVSHQLGSLMDLFTTSLALAG 326
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
148-492 |
1.88e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 79.31 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 148 GEPPVSKPNIILIISDDQGVDASNQYSYSTDLpkTPILDSLATSGVVFDNAWAtPACTTTRG--TIMTGMHGVNSGvSFV 225
Cdd:COG1368 228 PFGPAKKPNVVVILLESFSDFFIGALGNGKDV--TPFLDSLAKESLYFGNFYS-QGGRTSRGefAVLTGLPPLPGG-SPY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 226 PAVMDTSLTTLPRFLAENDASKAYsmavfgkWHlgGGDP-----DLSHPNsAGVGHYVGnitgtLDDYSD-----WTLTD 295
Cdd:COG1368 304 KRPGQNNFPSLPSILKKQGYETSF-------FH--GGDGsfwnrDSFYKN-LGFDEFYD-----REDFDDpfdggWGVSD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 296 ngsqtqvtqyhtSKVTDLAMDWITQQTSPWFVWLAYVAPHSPFHLPPNElhtrSELSGSAEDIAQNprpyYLAAIEAMDT 375
Cdd:COG1368 369 ------------EDLFDKALEELEKLKKPFFAFLITLSNHGPYTLPEED----KKIPDYGKTTLNN----YLNAVRYADQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 376 EIGRLLASLptDER---ENTLVIFIGDNGTPAPvidtsvyarQHSKNSLYEGGIRVPLLVSGNLLnKQNTRESRLVNSTD 452
Cdd:COG1368 429 ALGEFIEKL--KKSgwyDNTIFVIYGDHGPRSP---------GKTDYENPLERYRVPLLIYSPGL-KKPKVIDTVGSQID 496
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1482818008 453 LYATIVQIAGGDITQVYnshSFYDTLFDVVPNP-SVRQYNY 492
Cdd:COG1368 497 IAPTLLDLLGIDYPSYY---AFGRDLLSPDTDPfAFRNGGF 534
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
155-462 |
2.13e-14 |
|
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: 73.87 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDdqGVDASNQYSYSTDLPKTPILDSLATSGVVFDNAWATpacTTTRGTI------MTGMHGVNSGVSFVPAV 228
Cdd:cd16015 1 PNVIVILLE--SFSDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSP---GFGGGTAngefevLTGLPPLPLGSGSYTLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 229 MDTSLTTLPRFLAENDaskaYSMAVFgkwhlgggdpdlsHPNSA------------GVGHYVG--NITGTLDDYSDWTLT 294
Cdd:cd16015 76 KLNPLPSLPSILKEQG----YETIFI-------------HGGDAsfynrdsvypnlGFDEFYDleDFPDDEKETNGWGVS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 295 DngsqtqvtqyhtSKVTDLAMDWITQQTS-PWFVWLAYVAPHSPFHLPPNELHTRSELSGSAEDIAQnprpyYLAAIEAM 373
Cdd:cd16015 139 D------------ESLFDQALEELEELKKkPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELEN-----YLNAIHYT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 374 DTEIGRLLASLPT-DERENTLVIFIGDNGtpaPVIDTSVYARQHSKNSLYeggiRVPLLVSGNLLnKQNTRESRLVNSTD 452
Cdd:cd16015 202 DKALGEFIEKLKKsGLYENTIIVIYGDHL---PSLGSDYDETDEDPLDLY----RTPLLIYSPGL-KKPKKIDRVGSQID 273
|
330
....*....|
gi 1482818008 453 LYATIVQIAG 462
Cdd:cd16015 274 IAPTLLDLLG 283
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
155-461 |
1.05e-12 |
|
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: 67.83 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDASNQYSYSTdlPKTPILDSLATSGVVFDNAWATPACTTT--RGTIMTGMHGVNSGVsfvpavmdts 232
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPA--PTTPNLKRLASEGATFNFRSVSPPTSSApnHAALLTGAYPTLHGY---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 233 lttlprflAENDASKAYSMAVFGKWHLGGGdpdlshpnsagvghyvgNITGTLDDysdwtltdngSQTQVTQYHTSKvtd 312
Cdd:cd00016 69 --------TGNGSADPELPSRAAGKDEDGP-----------------TIPELLKQ----------AGYRTGVIGLLK--- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 313 lAMDWITQQtSPWFVWLAYVAPHSPFHlppnelhtrselsgsaeDIAQNPRPYYlAAIEAMDTEIGRLLASLP-TDEREN 391
Cdd:cd00016 111 -AIDETSKE-KPFVLFLHFDGPDGPGH-----------------AYGPNTPEYY-DAVEEIDERIGKVLDALKkAGDADD 170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 392 TLVIFIGDNGtpAPVIDTSVYARQHSKNSLYEGGIRVPLLVSGNLLNKQNTrESRLVNSTDLYATIVQIA 461
Cdd:cd00016 171 TVIIVTADHG--GIDKGHGGDPKADGKADKSHTGMRVPFIAYGPGVKKGGV-KHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
155-535 |
2.90e-11 |
|
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: 65.72 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 155 PNIILIISDDQGVDA----SNQYSYstdlpkTPILDSLATSGVVFDNAWAT-PACTTTRGTIMTG--MHgVNsGVSFVPA 227
Cdd:cd16150 1 PNIVIFVADQLRADSlghlGNPAAV------TPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGwyPH-VN-GHRTLHH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 228 VMDTSLTTLPRFLAENdaskAYSMAVFGKWHlgggdpDLSHPNSAGvghyvgnitgtldDYSDWtltDngsqtqvtqyht 307
Cdd:cd16150 73 LLRPDEPNLLKTLKDA----GYHVAWAGKND------DLPGEFAAE-------------AYCDS---D------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 308 SKVTDLAMDWITQQTS--PWFVWLAYVAPHSPF-------------HLPPN--------------ELHTRSELSGSAEDI 358
Cdd:cd16150 115 EACVRTAIDWLRNRRPdkPFCLYLPLIFPHPPYgveepwfsmidreKLPPRrppglrakgkpsmlEGIEKQGLDRWSEER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 359 AQNPRPYYLAAIEAMDTEIGRLLASL-PTDERENTLVIFIGDNGTpapvidtsvYARQHS-----KNSLYEGGIRVPLLV 432
Cdd:cd16150 195 WRELRATYLGMVSRLDHQFGRLLEALkETGLYDDTAVFFFSDHGD---------YTGDYGlvekwPNTFEDCLTRVPLII 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1482818008 433 SGNLLNKQNTRESrLVNSTDLYATIVQIAGGDITQVYNSHSFYDTLFDvvPNPSVRQYNYAD----------FQRNGV-- 500
Cdd:cd16150 266 KPPGGPAGGVSDA-LVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAG--ETEEHRDAVFSEggrlhgeeqaMEGGHGpy 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1482818008 501 -----------------AGWAVRNQDYKLLSIDSQQQALFDMNVDINEQNDL 535
Cdd:cd16150 343 dlkwprllqqeeppehtKAVMIRTRRYKYVYRLYEPDELYDLEADPLELHNL 394
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
364-401 |
2.68e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 40.12 E-value: 2.68e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1482818008 364 PYYLAAIEAMDTEIGRLLASLP-TDERENTLVIFIGDNG 401
Cdd:COG1524 205 PEYRAALREVDAALGRLLDALKaRGLYEGTLVIVTADHG 243
|
|
| |
