|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
45-555 |
0e+00 |
|
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: 619.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGNY 124
Cdd:cd16030 3 PNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAPDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKVFHPGVSSNysDDYPYSWSIPPFHPSAEKHENDKTCRGKDGKLHANLVCPVNVTEMPEGTL 204
Cdd:cd16030 83 VTLPQYFKENGYTTAGVGKIFHPGIPDG--DDDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGGGGPAWEAADVPDEAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 205 PDIQSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLaPDPWVPKKLPSVAYNPWVDIRQRDDV 284
Cdd:cd16030 161 PDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPFDPIDLPEVAWNDLDDLPKYGDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 285 EALNVSFPYGALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSNFDVATR 364
Cdd:cd16030 240 PALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHGHWGKHTLFEEATR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 365 VPLIFYVPGMTTspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRVPPacpemsfgvalCTEGRS 444
Cdd:cd16030 320 VPLIIRAPGVTK-----------------------PGKVTDALVELVDIYPTLAELAGLPAPP-----------CLEGKS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 445 IVHYFnisKGEVGEGKEgcvdtdrcfneepVAFSQYPRPAdtpqwnsdkpklkdirIMGYSMRTIDYRYTLWVqfdpnnf 524
Cdd:cd16030 366 LVPLL---KNPSAKWKD-------------AAFSQYPRPS----------------IMGYSIRTERYRYTEWV------- 406
|
490 500 510
....*....|....*....|....*....|.
gi 2043871144 525 saNFKDVHAGELYMMENDPNQDYNVYNNTSH 555
Cdd:cd16030 407 --DFDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
46-552 |
1.55e-91 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 286.39 E-value: 1.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVH-AGN 123
Cdd:COG3119 25 NILFILADDLGYgDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGlPPD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 YSTMPQYFKENGYVTLSVGKVFHpgvssnYSDDYpyswsippfhpsaekhendktcrgkdgklhanlvcpvnvtempegt 203
Cdd:COG3119 105 EPTLAELLKEAGYRTALFGKWHL------YLTDL---------------------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 204 lpdiqSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLaPDPWVPKklpsvaynpwvdirqrdd 283
Cdd:COG3119 133 -----LTDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-PPNLAPR------------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 284 vealnvsfpygALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHG-EWAKYSNFDVA 362
Cdd:COG3119 189 -----------DLTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGlRGGKGTLYEGG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 363 TRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELVSLFPTLAELAGLRVPPACpemsfgvalctE 441
Cdd:COG3119 258 IRVPLIVRWPGK------------------------IKAGSvSDALVSLIDLLPTLLDLAGVPIPEDL-----------D 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 442 GRSIVHYFnisKGEVGEGKEgcvdtdrcfneepVAFSQYPRPAdtpqwnsdkpklkdiriMGYSMRTIDYRYTLWvqfdp 521
Cdd:COG3119 303 GRSLLPLL---TGEKAEWRD-------------YLYWEYPRGG-----------------GNRAIRTGRWKLIRY----- 344
|
490 500 510
....*....|....*....|....*....|.
gi 2043871144 522 nnfsanFKDVHAGELYMMENDPNQDYNVYNN 552
Cdd:COG3119 345 ------YDDDGPWELYDLKNDPGETNNLAAD 369
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-544 |
9.98e-62 |
|
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: 206.24 E-value: 9.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWrvhAGN 123
Cdd:cd16037 1 PNILIIMSDEHNPdAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPY---DGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 YSTMPQYFKENGYVTLSVGKVfHpgvssnysddypyswsippFHPSAEKHendktcrgkdgklhanlvcpvnvtempeGT 203
Cdd:cd16037 78 VPSWGHALRAAGYETVLIGKL-H-------------------FRGEDQRH----------------------------GF 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 204 LPDIQSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYplenitlapdpwvpkklpsvaynpwvdirqrdd 283
Cdd:cd16037 110 RYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY--------------------------------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 284 vealnvsfpygalpddfQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSNFDVAT 363
Cdd:cd16037 157 -----------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKSTMYEESV 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 364 RVPLIFYVPGmttspVSQGARVfpyldpfsyigvsvpqgqsKEVVELVSLFPTLAELAGLRVPPACPemsfgvalcteGR 443
Cdd:cd16037 220 RVPMIISGPG-----IPAGKRV-------------------KTPVSLVDLAPTILEAAGAPPPPDLD-----------GR 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 444 SIVhyfniskgEVGEGKEgcvDTDRcfneepVAFSQYPRpadtpqwnsdkpklKDIRIMGYSMRTIDYRYTLWVQFDPnn 523
Cdd:cd16037 265 SLL--------PLAEGPD---DPDR------VVFSEYHA--------------HGSPSGAFMLRKGRWKYIYYVGYPP-- 311
|
490 500
....*....|....*....|.
gi 2043871144 524 fsanfkdvhagELYMMENDPN 544
Cdd:cd16037 312 -----------QLFDLENDPE 321
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
45-555 |
1.93e-60 |
|
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: 204.66 E-value: 1.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGNY 124
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRGFPLPDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKVFHPGvssnysdDYPYSWSIPPFHPSAEKHENDKTCRGKDGKLHANlvcpvnvtemPEGtl 204
Cdd:cd16027 81 KTLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA----------KKG-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 205 pdiqsteeaihllnvmkttrQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITlapdpwVPKKLPsvaynpwvdirqrdDV 284
Cdd:cd16027 142 --------------------QPFFLWFGFHDPHRPYPPGDGEEPGYDPEKVK------VPPYLP--------------DT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 285 EALnvsfpygalpddfqRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGehgeWAKYSNFDVATR 364
Cdd:cd16027 182 PEV--------------REDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 365 VPLIFYVPGMTTspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRVPpacPEMsfgvalctEGRS 444
Cdd:cd16027 244 VPLIVRWPGKIK-----------------------PGSVSDALVSFIDLAPTLLDLAGIEPP---EYL--------QGRS 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 445 IvhyFNISKGEVGEGKEgcvdtdrcfneepVAFSQYPRpADtpqwnsdkpklkdirIMGYSMRTI---DYRYTLwvqfdp 521
Cdd:cd16027 290 F---LPLLKGEKDPGRD-------------YVFAERDR-HD---------------ETYDPIRSVrtgRYKYIR------ 331
|
490 500 510
....*....|....*....|....*....|....
gi 2043871144 522 nnfsaNFKDVhagELYMMENDPNQDYNVYNNTSH 555
Cdd:cd16027 332 -----NYMPE---ELYDLKNDPDELNNLADDPEY 357
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
46-426 |
3.01e-60 |
|
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: 199.59 E-value: 3.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGNY 124
Cdd:cd16022 2 NILLIMTDDLGYdDLGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLPPDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVgkvfhpgvssnysddypyswsippfhpsaekhendktcrgkdGKLHanlvcpvnvtempegtl 204
Cdd:cd16022 82 PTLAELLKEAGYRTALI------------------------------------------GKWH----------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 205 pdiqstEEAIHLLNvMKTTRQKFFLAVGYHKPHiplrypqeflklyplenitlapdpwvpkklpsvayNPWVdirqrddv 284
Cdd:cd16022 103 ------DEAIDFIE-RRDKDKPFFLYVSFNAPH-----------------------------------PPFA-------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 285 ealnvsfpygalpddfqrqirqsYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGE-WAKYSNFDVAT 363
Cdd:cd16022 133 -----------------------YYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLrGKKGSLYEGGI 189
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2043871144 364 RVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELVSLFPTLAELAGLRVP 426
Cdd:cd16022 190 RVPFIVRWPGK------------------------IPAGQvSDALVSLLDLLPTLLDLAGIEPP 229
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-429 |
4.54e-60 |
|
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: 203.57 E-value: 4.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQ----QAVCAPSRVSFLTGRrpdttrlydfySYWRVH 120
Cdd:cd16155 4 NILFILADDQRAdTIGALGNPEIQTPNLDRLARRGTSFTNAYNMggwsGAVCVPSRAMLMTGR-----------TLFHAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 121 AGNYS-------TMPQYFKENGYVTLSVGKvfhpgvssnysddypysWsippfHPSaekhendktcrgkdgklHANlvcp 193
Cdd:cd16155 73 EGGKAaipsddkTWPETFKKAGYRTFATGK-----------------W-----HNG-----------------FAD---- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 194 vnvtempegtlpdiqsteEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLAPDPwvpkkLPSVAYN 273
Cdd:cd16155 110 ------------------AAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENF-----LPQHPFD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 274 PwVDIRQRDDVEAlnvsfPYGALPDDFQRQIRQsYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEW 353
Cdd:cd16155 167 N-GEGTVRDEQLA-----PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLM 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043871144 354 AKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvsVPQGQS-KEVVELVSLFPTLAELAGLRVPPAC 429
Cdd:cd16155 240 GKQNLYEHSMRVPLIISGPG-------------------------IPKGKRrDALVYLQDVFPTLCELAGIEIPESV 291
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-551 |
4.14e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 202.07 E-value: 4.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLY----DFYSYWRV 119
Cdd:cd16033 1 PNILFIMTDQQRyDTLGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLnnveNAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 120 HAGNYSTMPQYFKENGYVTLSVGKvfhpgvssnysddypysWsippfHPSAEKHENDktcRGKDGklhanlVCPVNVTEm 199
Cdd:cd16033 81 LPPGVETFSEDLREAGYRNGYVGK-----------------W-----HVGPEETPLD---YGFDE------YLPVETTI- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 200 pEGTLpdiqsTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLAP---DPWVPKklPSVAYNpwv 276
Cdd:cd16033 129 -EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPEsfaDDFEDK--PYIYRR--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 277 dIRQRDDVEALNvsfpygalpDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAK- 355
Cdd:cd16033 198 -ERKRWGVDTED---------EEDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKg 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 356 YSNFDVATRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELVSLFPTLAELAGLRVPPACpemsf 434
Cdd:cd16033 268 PFMYEETYRIPLIIKWPGV------------------------IAAGQvVDEFVSLLDLAPTILDLAGVDVPPKV----- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 435 gvalctEGRSIVhyfNISKGEVGEGkegcvdtdrcFNEEPVAfsqyprpadtpQWNSDKPKLkdiriMGYSMRTIDYRYT 514
Cdd:cd16033 319 ------DGRSLL---PLLRGEQPED----------WRDEVVT-----------EYNGHEFYL-----PQRMVRTDRYKYV 363
|
490 500 510
....*....|....*....|....*....|....*..
gi 2043871144 515 lwvqFDPNNFSanfkdvhagELYMMENDPNQDYNVYN 551
Cdd:cd16033 364 ----FNGFDID---------ELYDLESDPYELNNLID 387
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
45-562 |
6.94e-56 |
|
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: 193.90 E-value: 6.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGN 123
Cdd:cd16031 3 PNIIFILTDDHRyDALGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDASQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 ysTMPQYFKENGYVTLSVGKvFHPGVSSNYSD---DYPYSWSIPPFHPSAEKHENDKTcRGKDGklHANLVCpvnvtemp 200
Cdd:cd16031 83 --TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPpgfDYWVSFPGQGSYYDPEFIENGKR-VGQKG--YVTDII-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 201 egtlpdiqsTEEAIHLL-NVMKTtrQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLaPDPWVPKKLPSVAynPWVdiR 279
Cdd:cd16031 149 ---------TDKALDFLkERDKD--KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPE-PETFDDDDYAGRP--EWA--R 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 280 QRDDVEALNVSFPYGAlPDDFQRQIRQsYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGeWA-KYSN 358
Cdd:cd16031 213 EQRNRIRGVLDGRFDT-PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 359 FDVATRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELVSLFPTLAELAGLRVPPACpemsfgva 437
Cdd:cd16031 290 YEESIRVPLIIRDPRL------------------------IKAGTvVDALVLNIDFAPTILDLAGVPIPEDM-------- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 438 lctEGRSIVHYFniskgevgEGKEGcvDTDRcfneePVAFSQY---PRPADTPQWnsdkpklkdirimgYSMRTIDYRYT 514
Cdd:cd16031 338 ---QGRSLLPLL--------EGEKP--VDWR-----KEFYYEYyeePNFHNVPTH--------------EGVRTERYKYI 385
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2043871144 515 LWVQFDPNNfsanfkdvhagELYMMENDPNQDYNVYNNTSHGWFFKKL 562
Cdd:cd16031 386 YYYGVWDEE-----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-426 |
5.11e-54 |
|
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: 188.16 E-value: 5.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLydFYSYWRVHAgNY 124
Cdd:cd16034 3 NILFIFADQHRaQALGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV--FGNDVPLPP-DA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKvFHpgVSSNYSDDYPYSWSIPP---------------FHPSAEKHENDKtcrgkDGKLHAn 189
Cdd:cd16034 80 PTIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecNHDHNNPHYYDD-----DGKRIY- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 190 lvcpvnvtemPEGTLPDIQsTEEAIHLLNVMKTTRQKFFLAVGYHKPHIP-LRYPQEFLKLYPLENITLAPDpwvpkklp 268
Cdd:cd16034 151 ----------IKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPyTTAPEEYLDMYDPKKLLLRPN-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 269 svaynpwVDIRQRDDvealnvsfpygalpDDFQRQIRQsYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLG 348
Cdd:cd16034 212 -------VPEDKKEE--------------AGLREDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLG 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043871144 349 EHGEWAKYSNFDVATRVPLIFYVPGMttspvsqgarvFPYldpfsyiGVSVPQgqskeVVELVSLFPTLAELAGLRVP 426
Cdd:cd16034 270 SHGLMNKQVPYEESIRVPFIIRYPGK-----------IKA-------GRVVDL-----LINTVDIMPTLLGLCGLPIP 324
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
46-427 |
1.56e-53 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 189.11 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTT-RLydfySYWRVHAGN 123
Cdd:PRK13759 8 NIILIMVDQMRgDCLGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRV----GYGDVVPWN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 YS-TMPQYFKENGYVTLSVGKV-FHP------------------------GVSSNYSDDY-PYSWSIPPFH-PSAEKH-- 173
Cdd:PRK13759 84 YKnTLPQEFRDAGYYTQCIGKMhVFPqrnllgfhnvllhdgylhsgrnedKSQFDFVSDYlAWLREKAPGKdPDLTDIgw 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 174 -ENDKTCR--GKDGKLHanlvcPVNVTempegtlpdiqsTEEAIHLLNvMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLY 250
Cdd:PRK13759 164 dCNSWVARpwDLEERLH-----PTNWV------------GSESIEFLR-RRDPTKPFFLKMSFARPHSPYDPPKRYFDMY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 251 PLENItlaPDPWVpkklpsvayNPWvDIRQRDDVEALNVSFPYGALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAG 330
Cdd:PRK13759 226 KDADI---PDPHI---------GDW-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 331 LSNNTIVVFTADHGWSLGEHGEWAKYSNFDVATRVPLIFYVPGMTTSPvsqgarvfpyldpfsyigvsvPQGQ-SKEVVE 409
Cdd:PRK13759 293 LLDNTIILFVSDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAG---------------------NRGTvIDQVVE 351
|
410
....*....|....*...
gi 2043871144 410 LVSLFPTLAELAGLRVPP 427
Cdd:PRK13759 352 LRDIMPTLLDLAGGTIPD 369
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
46-446 |
5.58e-52 |
|
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: 180.47 E-value: 5.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWrvhAGNY 124
Cdd:cd16032 2 NILLIMADQLTAaALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDNAAEF---PADI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKV-F-----HPGVSsnYSDDYPYSwsippfhpsAEKHENDKTcRGKDGKlhanlvcpvnvte 198
Cdd:cd16032 79 PTFAHYLRAAGYRTALSGKMhFvgpdqLHGFD--YDEEVAFK---------AVQKLYDLA-RGEDGR------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 199 mpegtlPdiqsteeaihllnvmkttrqkFFLAVGYHKPHIPLRYPQEFLKLYplenitlapdpwvpkklpsvaynpwvdi 278
Cdd:cd16032 134 ------P---------------------FFLTVSFTHPHDPYVIPQEYWDLY---------------------------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 279 rqrddvealnvsfpygalpddfQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSN 358
Cdd:cd16032 159 ----------------------VRRARRAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSF 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 359 FDVATRVPLIFYVPGmttspVSQGARVfpyldpfsyigvsvpqgqsKEVVELVSLFPTLAELAGLRVPPACPEMsfgval 438
Cdd:cd16032 217 FEGSARVPLIISAPG-----RFAPRRV-------------------AEPVSLVDLLPTLVDLAGGGTAPHVPPL------ 266
|
....*...
gi 2043871144 439 ctEGRSIV 446
Cdd:cd16032 267 --DGRSLL 272
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-427 |
1.98e-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: 293763 [Multi-domain] Cd Length: 421 Bit Score: 179.28 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL-RPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGNY 124
Cdd:cd16144 2 NIVLILVDDLgWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 S---------------TMPQYFKENGYVTLSVGKvFH-PGVSSNYSDDYPYSWSIPPFHPSAekhendktcrGKDGKLHA 188
Cdd:cd16144 82 KlipppsttrlpleevTIAEALKDAGYATAHFGK-WHlGGEGGYGPEDQGFDVNIGGTGNGG----------PPSYYFPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 189 NLVCPVNVTEMPEGTLPDiQSTEEAIhllNVMKTTRQK-FFLAVGYHKPHIPLRYPQEFLKLYPlenitlapdpwvpkkl 267
Cdd:cd16144 151 GKPNPDLEDGPEGEYLTD-RLTDEAI---DFIEQNKDKpFFLYLSHYAVHTPIQARPELIEKYE---------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 268 psvaynpwvdirqrddvealnvsfpygALPDDFQRQIRQSYYAA-VSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGwS 346
Cdd:cd16144 211 ---------------------------KKKKGLRKGQKNPVYAAmIESLDESVGRILDALEELGLADNTLVIFTSDNG-G 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 347 LGEHGEWA---------KYSNFDVATRVPLIFYVPGMTTspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTL 417
Cdd:cd16144 263 LSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK-----------------------PGSVSDVPVIGTDLYPTF 319
|
410
....*....|
gi 2043871144 418 AELAGLRVPP 427
Cdd:cd16144 320 LELAGGPLPP 329
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-427 |
2.33e-48 |
|
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: 169.27 E-value: 2.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPdttrlydfySYWRVHAGN 123
Cdd:cd16148 1 MNVILIVIDSLRAdHLGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYP---------FYHGVWGGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 YS----TMPQYFKENGYVTLsvgkvfhpGVSSNysddyPYSWSIPPFHPSAEKHENDktcRGKDGKLHanlvcpvnvtem 199
Cdd:cd16148 72 LEpddpTLAEILRKAGYYTA--------AVSSN-----PHLFGGPGFDRGFDTFEDF---RGQEGDPG------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 200 PEGTLPDIQSTEEAIHLLNVMKTTRqKFFLAVGYHKPHIPLRypqeflklyplenitlapdpwvpkklpsvaynpwvdir 279
Cdd:cd16148 124 EEGDERAERVTDRALEWLDRNADDD-PFFLFLHYFDPHEPYL-------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 280 qrddvealnvsfpygalpddfqrqirqsYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAK-YSN 358
Cdd:cd16148 165 ----------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGhGSN 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 359 F-DVATRVPLIFYVPGMTtspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRVPP 427
Cdd:cd16148 217 LyDEQLHVPLIIRWPGKE------------------------PGKRVDALVSHIDIAPTLLDLLGVEPPD 262
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
45-429 |
3.23e-48 |
|
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: 173.98 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRrpdttrlydfysYWRVH--- 120
Cdd:cd16028 1 RNVLFITADQWRaDCLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGR------------YLMNHrsv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 121 ------AGNYSTMPQYFKENGYVTLSVGkvfhpgvssnYSDDYPYSWSIPPFHPSaekhendktcrgkdgKLHANLVCP- 193
Cdd:cd16028 69 wngtplDARHLTLALELRKAGYDPALFG----------YTDTSPDPRGLAPLDPR---------------LLSYELAMPg 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 194 ----VNVTEMPEGTLPDIQSTEEAIHLLNVMKttRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITL-----------A 258
Cdd:cd16028 124 fdpvDRLDEYPAEDSDTAFLTDRAIEYLDERQ--DEPWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpiraeslaaeaA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 259 PDPWvpkklpsvaYNPWVDIRQRDDVEAlnVSFPYGALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVV 338
Cdd:cd16028 202 QHPL---------LAAFLERIESLSFSP--GAANAADLDDEEVAQMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 339 FTADHGWSLGEHGEWAKYSNFDVATRVPLIFYVPGMTTSPvSQGARVfpylDPFsyigvsvpqgqskevVELVSLFPTLA 418
Cdd:cd16028 271 FTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREADA-TRGQVV----DAF---------------TESVDVMPTIL 330
|
410
....*....|.
gi 2043871144 419 ELAGLRVPPAC 429
Cdd:cd16028 331 DWLGGEIPHQC 341
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-566 |
9.82e-47 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 169.34 E-value: 9.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGN 123
Cdd:cd16150 1 PNIVIFVADQLRAdSLGHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNGHRTLHHLLRPDEPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 ystMPQYFKENGYVTLSVGKvfhpgvssnySDDYPyswsippfhpsaEKHENDKTCrgkdgklhanlvcpvnvtempegt 203
Cdd:cd16150 81 ---LLKTLKDAGYHVAWAGK----------NDDLP------------GEFAAEAYC------------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 204 LPDIQSTEEAIHLLNvMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLEnitLAPDPWVPKKLpsvAYNPwVDIRQRDD 283
Cdd:cd16150 112 DSDEACVRTAIDWLR-NRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLPPRRPPGLR---AKGK-PSMLEGIE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 284 VEALNvsfpygALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSN-F-DV 361
Cdd:cd16150 184 KQGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeDC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 362 ATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvSVPQGQSKEVVELVSLFPTLAELAGLRVPPAcpemSFGVALCte 441
Cdd:cd16150 258 LTRVPLIIKPPG------------------------GPAGGVSDALVELVDIPPTLLDLAGIPLSHT----HFGRSLL-- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 442 grsivhyfNISKGEVGEGKegcvdtDRCFNE------EPVAFSQYPRPADtPQWNSDKPKLK-DIRIMGYSMRTIDYRYt 514
Cdd:cd16150 308 --------PVLAGETEEHR------DAVFSEggrlhgEEQAMEGGHGPYD-LKWPRLLQQEEpPEHTKAVMIRTRRYKY- 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2043871144 515 LWVQFDPNnfsanfkdvhagELYMMENDPNQDYNVYNNTSHG----WFFKKLLGFL 566
Cdd:cd16150 372 VYRLYEPD------------ELYDLEADPLELHNLIGDPAYAeiiaEMKQRLLRWM 415
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-425 |
2.81e-44 |
|
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: 158.69 E-value: 2.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKL----------VKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFY 114
Cdd:cd16153 3 NILWIITDDQRVdSLSCYNNAHtgksesrlgyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 115 SYWRVHAGNYSTMPQYFKENGYVTLSVGKvfhpgvssnysddypyswsippfhpsaEKHENdktcrgkdgklhanlvcPV 194
Cdd:cd16153 83 AAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA-----------------FQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 195 NVTEMPegtlpdIQSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLrypqeflklyplenitLAPDPWvpkklpsvaynp 274
Cdd:cd16153 119 RYLKNA------NQSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPV----------------LPPKEF------------ 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 275 wvdiRQRDDvealnvsfpygalpddfqrqirqsYYAAVSYLDVQIGLLLSALDDAGLSN---NTIVVFTADHGWSLGEHG 351
Cdd:cd16153 165 ----RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYVTGDHGWHLGEQG 216
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2043871144 352 EWAKYSNFDVATRVPLIFyvpgmttspVSQGARVFPyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRV 425
Cdd:cd16153 217 ILAKFTFWPQSHRVPLIV---------VSSDKLKAP------------AGKVRHDFVEFVDLAPTLLAAAGVDV 269
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-426 |
4.16e-43 |
|
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: 158.50 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLrp-vLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSywrVHAGNY 124
Cdd:cd16026 3 NIVVILADDLgygdLGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVRVGLPGVVG---PPGSKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 S------TMPQYFKENGYVTLSVGKvFHPGVSSNYS------DDY---PYSWSIPPFHPSAEKHENDKtcrgkdgklhAN 189
Cdd:cd16026 80 GlppdeiTIAEVLKKAGYRTALVGK-WHLGHQPEFLptrhgfDEYfgiPYSNDMWPFPLYRNDPPGPL----------PP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 190 LVCPVNVTEMPegtlPDiQS------TEEAIHLLnvmktTRQK---FFLAVGYHKPHIPLRYPQEFlklyplenitlapd 260
Cdd:cd16026 149 LMENEEVIEQP----AD-QSsltqryTDEAVDFI-----ERNKdqpFFLYLAHTMPHVPLFASEKF-------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 261 pwvpkklpsvaynpwvdirqRDDVEAlnvsFPYGalpddfqrqirqsyyAAVSYLDVQIGLLLSALDDAGLSNNTIVVFT 340
Cdd:cd16026 205 --------------------KGRSGA----GLYG---------------DVVEELDWSVGRILDALKELGLEENTLVIFT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 341 ADHGWSLGEHGEW--------AKYSNFDVATRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELV 411
Cdd:cd16026 246 SDNGPWLEYGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTvSDELASTM 301
|
410
....*....|....*
gi 2043871144 412 SLFPTLAELAGLRVP 426
Cdd:cd16026 302 DLLPTLAALAGAPLP 316
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-426 |
2.42e-41 |
|
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: 154.29 E-value: 2.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHA--G 122
Cdd:cd16145 2 NIIFILADDLGYgDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPlpP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 123 NYSTMPQYFKENGYVTLSVGK-----VFHPGVSSNYSDDYPYSWS--------IPPFhpsaeKHENDKTcRGKDGKLHAN 189
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKwglggPGTPGHPTKQGFDYFYGYLdqvhahnyYPEY-----LWRNGEK-VPLPNNVIPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 190 LVCPVNVTEMPEGTLPDIqSTEEAihlLNVMKTTRQK-FFLAVGYHKPHIPLRYPQeflklyplenitLAPDPWVPKKLP 268
Cdd:cd16145 156 LDEGNNAGGGGGTYSHDL-FTDEA---LDFIRENKDKpFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 269 SVAYNPWvdirqrddvealnvsfpygalpddfqRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLg 348
Cdd:cd16145 220 IYAYLPW--------------------------PQPEKAYAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNGPHS- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 349 EHGEWAKYSNFDVA--------------TRVPLIFYVPGmttspvsqgarvfpyldpfsyigvSVPQGQ-SKEVVELVSL 413
Cdd:cd16145 273 EGGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPG------------------------KIPAGSvSDHPSAFWDF 328
|
410
....*....|...
gi 2043871144 414 FPTLAELAGLRVP 426
Cdd:cd16145 329 MPTLADLAGAEPP 341
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
46-549 |
3.81e-41 |
|
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: 153.47 E-value: 3.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL-RPVLGCYGDKLVKSPNIDQLASQSMVFSNAYaQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGNY 124
Cdd:cd16146 2 NVILILTDDQgYGDLGFHGNPILKTPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGVWHTILGRERMRLDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKvFHPGvssnysDDYPYswsippfHPsaekheNDktcRGKD-----------------GKLH 187
Cdd:cd16146 81 TTLAEVFKDAGYRTGIFGK-WHLG------DNYPY-------RP------QD---RGFDevlghggggigqypdywGNDY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 188 ANLVCPVNVTEMP-EGTLPDIQsTEEAIhllNVMKTTRQK-FFLAVGYHKPHIPLRYPQEFLKLYplenitlapdpwvpK 265
Cdd:cd16146 138 FDDTYYHNGKFVKtEGYCTDVF-FDEAI---DFIEENKDKpFFAYLATNAPHGPLQVPDKYLDPY--------------K 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 266 KLpsvaynpwvdirqrddvealnvsfpygALPDDfqrqiRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGW 345
Cdd:cd16146 200 DM---------------------------GLDDK-----LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 346 SLGEHGEW------AKYSNFDVATRVPLIFYVPGMTTspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAE 419
Cdd:cd16146 248 AGGVPKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL-----------------------AGKDVDTLTAHIDLLPTLLD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 420 LAGLRVPPacpemsfGVALctEGRSIVHYfnISKGEVGEgkegcvdtdrcfnEEPVAFSQYPRPADTPQWNsdkpklkdi 499
Cdd:cd16146 305 LCGVKLPE-------GIKL--DGRSLLPL--LKGESDPW-------------PERTLFTHSGRWPPPPKKK--------- 351
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2043871144 500 riMGYSMRTIDYRYTlwvqfdpNNFSANFkdvhagELYMMENDPNQDYNV 549
Cdd:cd16146 352 --RNAAVRTGRWRLV-------SPKGFQP------ELYDIENDPGEENDV 386
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-434 |
6.95e-40 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 145.84 E-value: 6.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRV---- 119
Cdd:cd16149 1 PNILFILTDDQGPwALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHgktk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 120 HAGNY----STMPQYFKENGYVTLSVGKvFHPGvssnysddypyswsippfhpsaekhendktcrgkdgklhanlvcpvn 195
Cdd:cd16149 81 KPEGYlegqTTLPEVLQDAGYRCGLSGK-WHLG----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 196 vtempegtlpdiqsTEEAIHLLNVmKTTRQKFFLAVGYHKPHiplrypqeflklyplenitlapDPWvpkklpsvaynpw 275
Cdd:cd16149 113 --------------DDAADFLRRR-AEAEKPFFLSVNYTAPH----------------------SPW------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 276 vdirqrddvealnvsfpygalpddfqrqirqSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAK 355
Cdd:cd16149 143 -------------------------------GYFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGK 191
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 356 ------YSNFDVATRVPLIFYVPGMTTspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRVP--P 427
Cdd:cd16149 192 gngtfpLNMYDNSVKVPFIIRWPGVVP-----------------------AGRVVDSLVSAYDFFPTLLELAGVDPPadP 248
|
....*..
gi 2043871144 428 ACPEMSF 434
Cdd:cd16149 249 RLPGRSF 255
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
46-423 |
4.48e-37 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 139.48 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDfySYWRVHAGNY 124
Cdd:pfam00884 2 NVVLVLGESLRaPDLGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYV--STPVGLPRTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLsvgkVFHPGVSSNYSDDYPYswsippfhpsaeKHENDKTCRGkdGKLHANLV-CPVNVTEMPEGT 203
Cdd:pfam00884 80 PSLPDLLKRAGYNTG----AIGKWHLGWYNNQSPC------------NLGFDKFFGR--NTGSDLYAdPPDVPYNCSGGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 204 LPDIQSTEEAIHLLNVMKttrQKFFLAVGYHKPHIPLRYPQEFLKLYPlenitlapdpwvpkklpsvaynpwvdirqrdd 283
Cdd:pfam00884 142 VSDEALLDEALEFLDNND---KPFFLVLHTLGSHGPPYYPDRYPEKYA-------------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 284 vealnVSFPYgalpDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSNFDVA- 362
Cdd:pfam00884 187 -----TFKPS----SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYDNAp 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2043871144 363 ---TRVPLIFYVPGMTtspvsqgarvfpyldpfsyigvsVPQGQSKEVVELVSLFPTLAELAGL 423
Cdd:pfam00884 258 eggYRVPLLIWSPGGK-----------------------AKGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-489 |
1.45e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 140.04 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAqQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHagny 124
Cdd:cd16151 2 NIILIMADDLGYeCIGCYGGESYKTPNIDALAAEGVRFNNAYA-QPLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 sTMPQYFKENGYVTLSVGKvfhPGVSSNYSD-DYPyswsippfhpsaEKHENDKTC------RGKDGKLHANLVCPVNVT 197
Cdd:cd16151 77 -TFGHLLKDAGYATAIAGK---WQLGGGRGDgDYP------------HEFGFDEYClwqlteTGEKYSRPATPTFNIRNG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 198 EMPEGTL----PDIQSTeeaiHLLNVMKTTRQKFFLAvgYhkphiplrYPqeflklyplenITLAPDPWVPKKLPSVAYn 273
Cdd:cd16151 141 KLLETTEgdygPDLFAD----FLIDFIERNKDQPFFA--Y--------YP-----------MVLVHDPFVPTPDSPDWD- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 274 pwvdirqrddvealnvsfpygalPDDFQRQIRQSYYAA-VSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGE 352
Cdd:cd16151 195 -----------------------PDDKRKKDDPEYFPDmVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 353 W-------AKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvSVPQGQ-SKEVVELVSLFPTLAELAGLR 424
Cdd:cd16151 252 TngrevrgGKGKTTDAGTHVPLIVNWPG------------------------LIPAGGvSDDLVDFSDFLPTLAELAGAP 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043871144 425 VPPACPemsfgvalcTEGRSIVHYFniskgevgEGKEGcvdTDR----CFNEEPVAFSQYPRPADTPQW 489
Cdd:cd16151 308 LPEDYP---------LDGRSFAPQL--------LGKTG---SPRrewiYWYYRNPHKKFGSRFVRTKRY 356
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-434 |
3.10e-33 |
|
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: 131.17 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDK-LVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLydFYSYWRVHAGN 123
Cdd:cd16143 2 NIVIILADDLGYgDISCYNPDsKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRL--KGGVLGGFSPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 Y-----STMPQYFKENGYVTLSVGKvFHPGvssnysddypYSWSIPPFHPSAEKHENDKTCRG--KDGKLH--------- 187
Cdd:cd16143 80 LiepdrVTLAKMLKQAGYRTAMVGK-WHLG----------LDWKKKDGKKAATGTGKDVDYSKpiKGGPLDhgfdyyfgi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 188 -ANLVcpvnvtempegtLPDIqsTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLrypqeflklyplenitLAPDPWVPKK 266
Cdd:cd16143 149 pASEV------------LPTL--TDKAVEFIDQHAKKDKPFFLYFALPAPHTPI----------------VPSPEFQGKS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 267 LPSvaynpwvdirqrddvealnvsfPYGalpdDFqrqIRQsyyaavsyLDVQIGLLLSALDDAGLSNNTIVVFTADHG-- 344
Cdd:cd16143 199 GAG----------------------PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGps 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 345 -----WSLGEHGEWA-------KYSNFDVATRVPLIFYVPGMTtspvsqgarvfpyldpfsyigvsVPQGQSKEVVELVS 412
Cdd:cd16143 242 pyadyKELEKFGHDPsgplrgmKADIYEGGHRVPFIVRWPGKI-----------------------PAGSVSDQLVSLTD 298
|
410 420
....*....|....*....|..
gi 2043871144 413 LFPTLAELAGLRVPPACPEMSF 434
Cdd:cd16143 299 LFATLAAIVGQKLPDNAAEDSF 320
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
46-553 |
4.24e-33 |
|
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: 130.75 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRPVLGCYGD--KLVKspnidQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRP------DTTRLYDFYSYW 117
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPmpKTKK-----LLADQGTTFTNAFVTTPLCCPSRASILTGQYAhnhgvtNNSPPGGGYPKF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 118 RVHAGNYSTMPQYFKENGYVTLSVGKVFHPGVSSNYSDDYP--YSWSIPPFHPSaeKHENDKTCRGKDGKLHANLvcpvn 195
Cdd:cd16147 78 WQNGLERSTLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPpgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVSY----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 196 vtemPEGTLPDIqSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPleNITLAPDPwvPKKLPSVAYNP- 274
Cdd:cd16147 151 ----PGDYLTDV-IANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPRP--PPNNPDVSDKPh 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 275 WVDIRQRDDVEALNVSfpygalpDDFQRQIRQSYyAAVsylDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHG-EW 353
Cdd:cd16147 222 WLRRLPPLNPTQIAYI-------DELYRKRLRTL-QSV---DDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRlPP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 354 AKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvsVPQGQ-SKEVVELVSLFPTLAELAGLRVPpacPEM 432
Cdd:cd16147 291 GKRTPYEEDIRVPLLVRGPG-------------------------IPAGVtVDQLVSNIDLAPTILDLAGAPPP---SDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 433 sfgvalctEGRSIVHYFNiskgevgegkegcvDTDRCfneepvafsqyprpadtpqwnsdkpklkdirimgysMRTIDYR 512
Cdd:cd16147 343 --------DGRSCGDSNN--------------NTYKC------------------------------------VRTVDDT 364
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2043871144 513 YTLWVQFDPNNFSanfkdvhagELYMMENDPNQDYNVYNNT 553
Cdd:cd16147 365 YNLLYFEWCTGFR---------ELYDLTTDPYQLTNLAGDL 396
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
46-427 |
5.06e-32 |
|
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: 127.67 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLrpvlGcYGD------KLVKSPNIDQLASQSMVFSNAYAQQaVCAPSRVSFLTGRRPDTTRLYDFYSYWRV 119
Cdd:cd16029 2 HIVFILADDL----G-WNDvgfhgsDQIKTPNLDALAADGVILNNYYVQP-ICTPSRAALMTGRYPIHTGMQHGVILAGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 120 HAG---NYSTMPQYFKENGYVTLSVGKvFHPGVssnysddypYSWSIPP----------FHPSAEKHENDKTCRGKDgkl 186
Cdd:cd16029 76 PYGlplNETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGAND--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 187 hanlvCPVNVTEMPEGTLPDIQS-------TEEAIHLLNvMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPlenitlap 259
Cdd:cd16029 143 -----YGNDDLRDNEEPAWDYNGtystdlfTDRAVDIIE-NHDPSKPLFLYLAFQAVHAPLQVPPEYADPYE-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 260 dpwvpkklpsvaynpwvdirqrddvealnVSFPYGALPDdfqrqiRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVF 339
Cdd:cd16029 209 -----------------------------DKFAHIKDED------RRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 340 TADHGwslG--EHGEWA--------KYSNFDVATRvplifyVPGMTTSPVSQGARvfpyldpfsyigvsvpQGQSKEVVE 409
Cdd:cd16029 254 TSDNG---GptGGGDGGsnyplrggKNTLWEGGVR------VPAFVWSPLLPPKR----------------GTVSDGLMH 308
|
410
....*....|....*...
gi 2043871144 410 LVSLFPTLAELAGLRVPP 427
Cdd:cd16029 309 VTDWLPTLLSLAGGDPDD 326
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
46-450 |
7.50e-31 |
|
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: 124.48 E-value: 7.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDkLVKSPNIDQLASQSMVFSNAYAQqAVCAPSRVSFLTGR---------RPDTTRLYDFY- 114
Cdd:cd16025 4 NILLILADDLGFsDLGCFGG-EIPTPNLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRnhhqvgmgtMAELATGKPGYe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 115 SYWRVHAGnysTMPQYFKENGYVTLSVGKvFHPGvssnySDDYpYSwsippfhpsaekhendktcrgkdgklhanlvcpv 194
Cdd:cd16025 82 GYLPDSAA---TIAEVLKDAGYHTYMSGK-WHLG-----PDDY-YS---------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 195 nvTEmpegtlpDIqsTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFLKLY------------------------ 250
Cdd:cd16025 118 --TD-------DL--TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYkgkydagwdalreerlerqkelgl 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 251 -PlENITLAP-DPWVPkklpsvaynPWvdirqrDDvealnvsfpygaLPDDfQRQI---RQSYYAA-VSYLDVQIGLLLS 324
Cdd:cd16025 187 iP-ADTKLTPrPPGVP---------AW------DS------------LSPE-EKKLearRMEVYAAmVEHMDQQIGRLID 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 325 ALDDAGLSNNTIVVFTADHGWSlGEHGeWA----------KYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsy 394
Cdd:cd16025 238 YLKELGELDNTLIIFLSDNGAS-AEPG-WAnasntpfrlyKQASHEGGIRTPLIVSWPK--------------------- 294
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2043871144 395 iGVSVPQGQSKEVVELVSLFPTLAELAGlrVPPacPEMSFGVALCT-EGRSIVHYFN 450
Cdd:cd16025 295 -GIKAKGGIRHQFAHVIDIAPTILELAG--VEY--PKTVNGVPQLPlDGVSLLPTLD 346
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-468 |
8.13e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 120.80 E-value: 8.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRP-VLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTrlydfySYWR---VHA 121
Cdd:cd16152 3 NVIVFFTDQQRWdTLGCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTET------GCFRngiPLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 122 GNYSTMPQYFKENGYVTLSVGKvfhpgvssnysddypysWsippfHPSaeKHENDKTcrgkdgklhanlvcpvnvtempe 201
Cdd:cd16152 77 ADEKTLAHYFRDAGYETGYVGK-----------------W-----HLA--GYRVDAL----------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 202 gtlpdiqsTEEAIHLLNvMKTTRQKFFLAVGYHKPHI---------PLRYPQEFlklyplenitlaPDPWVPKKLpsvay 272
Cdd:cd16152 110 --------TDFAIDYLD-NRQKDKPFFLFLSYLEPHHqndrdryvaPEGSAERF------------ANFWVPPDL----- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 273 npwvdirqrddvealnvsfpyGALPDDFQRQIrQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHgwslGEH-- 350
Cdd:cd16152 164 ---------------------AALPGDWAEEL-PDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfr 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 351 ---GEWaKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpFSYIGVSVpqgqskEVVELVSLFPTLAELAGLRVPp 427
Cdd:cd16152 218 trnAEY-KRSCHESSIRVPLVIYGPG------------------FNGGGRVE------ELVSLIDLPPTLLDAAGIDVP- 271
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2043871144 428 acPEMSfgvalcteGRSIVH-------------YFNISKGEVGEgkegCVDTDR 468
Cdd:cd16152 272 --EEMQ--------GRSLLPlvdgkvedwrnevFIQISESQVGR----AIRTDR 311
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
46-428 |
2.50e-26 |
|
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: 110.70 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDlrpV----LGCYGDKLV---KSPNIDQLASQSMVFSNAYAQQAvCAPSRVSFLTGRRPdttrlydfysywr 118
Cdd:cd16142 2 NILVILGDD---IgwgdLGCYGGGIGrgaPTPNIDRLAKEGLRFTSFYVEPS-CTPGRAAFITGRHP------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 119 VHAGNYS---------------TMPQYFKENGYVTLSVGKvFHPGvssnysdDYPYSWsippfhPSAekhendktcRGKD 183
Cdd:cd16142 65 IRTGLTTvglpgspgglppwepTLAELLKDAGYATAQFGK-WHLG-------DEDGRL------PTD---------HGFD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 184 gklhanlvcpvnvtEMpEGTLP---DIQSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPlrypqeflklyplenitlapd 260
Cdd:cd16142 122 --------------EF-YGNLYhtiDEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFP--------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 261 pwvpkKLPSvaynpwvdirqrddvealnvsfpygalpDDFQ-RQIRQSYYA-AVSYLDVQIGLLLSALDDAGLSNNTIVV 338
Cdd:cd16142 166 -----TLPS----------------------------PEFEgKSSGKGKYAdSMVELDDHVGQILDALDELGIADNTIVI 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 339 FTADHG-----WSLGEHGEW--AKYSNFDVATRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQG-QSKEVVEL 410
Cdd:cd16142 213 FTTDNGpeqdvWPDGGYTPFrgEKGTTWEGGVRVPAIVRWPGK------------------------IKPGrVSNEIVSH 268
|
410
....*....|....*...
gi 2043871144 411 VSLFPTLAELAGLRVPPA 428
Cdd:cd16142 269 LDWFPTLAALAGAPDPKD 286
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
46-427 |
8.88e-26 |
|
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: 110.55 E-value: 8.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLydfYSYWRVHAGNY 124
Cdd:cd16156 2 QFIFIMTDTQRwDMVGCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGS---WTNCMALGDNV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKvFH-------------PGVSSNY-----------SDDYPYSWSIPPFHPSAEKHENDKTcr 180
Cdd:cd16156 79 KTIGQRLSDNGIHTAYIGK-WHldggdyfgngicpQGWDPDYwydmrnyldelTEEERRKSRRGLTSLEAEGIKEEFT-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 181 gkdgklHANLVcpvnvtempegtlpdiqsTEEAIHLLNvmKTTRQKFFLAVGYHKPHIPLRYPQEFLKLYPLENITLAPD 260
Cdd:cd16156 156 ------YGHRC------------------TNRALDFIE--KHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGEN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 261 PWVP-KKLPSvAYNPWVDIRQRDDVEALNVSFPYgalpddfqrqirqsYYAAVSYLDVQIGLLLSALDDagLSNNTIVVF 339
Cdd:cd16156 210 AYDDlENKPL-HQRLWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADE--IAEDAWVIY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 340 TADHGWSLGEHGEWAK-YSNFDVATRVPLIFYVPGMTTSPVSQGArvfpyldPFSYIgvsvpqgqskevvelvSLFPTLA 418
Cdd:cd16156 273 TSDHGDMLGAHKLWAKgPAVYDEITNIPLIIRGKGGEKAGTVTDT-------PVSHI----------------DLAPTIL 329
|
....*....
gi 2043871144 419 ELAGLRVPP 427
Cdd:cd16156 330 DYAGIPQPK 338
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
45-423 |
1.69e-23 |
|
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: 101.13 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 45 MNVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAGN 123
Cdd:cd16035 1 PNILLILTDQERyPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDTLGSPMQPLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 124 YS--TMPQYFKENGYVTLSVGKvfhpgvssnysddypysWsippfHPSAekhendktcrgkdgklHANlvcpvnvtempE 201
Cdd:cd16035 81 PDvpTLGHMLRAAGYYTAYKGK-----------------W-----HLSG----------------AAG-----------G 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 202 GTLPDIQSTEEAIHLLNVMKTT---RQKFFLAVGYHKPHiplrypqeflklyplenitlapdpwvpkklpsvaynpwvDI 278
Cdd:cd16035 112 GYKRDPGIAAQAVEWLRERGAKnadGKPWFLVVSLVNPH---------------------------------------DI 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 279 rqrddvealnvSFPygalPDDFQRQIRQS--YYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKY 356
Cdd:cd16035 153 -----------MFP----PDDEERWRRFRnfYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKG 217
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043871144 357 SN-FDVATRVPLIFYVPgmttspvsqgaRVFPyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGL 423
Cdd:cd16035 218 FNaYEEALHVPLIISHP-----------DLFG------------TGQTTDALTSHIDLLPTLLGLAGV 262
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
46-427 |
3.00e-22 |
|
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: 98.77 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRPVLGCY-GDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYsywRVHAGNY 124
Cdd:cd16171 2 NVVMVMSDSFDGRLTFRpGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNY---KGLDPNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLSVGKVFHpgVSSNYS-DDYPYSWSIP-PFhpsaekhendkTCRgKDGKLHANLVCPVNVTEMpeg 202
Cdd:cd16171 79 PTWMDRLEKHGYHTQKYGKLDY--TSGHHSvSNRVEAWTRDvPF-----------LLR-QEGRPTVNLVGDRSTVRV--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 203 TLPDIQSTEEAIH-LLNVMKTTRQKFFLAVGYHKPHiplrypqeflklyplenitlapdpwvPKKLPSVAYNpwvdirqr 281
Cdd:cd16171 142 MLKDWQNTDKAVHwIRKEAPNLTQPFALYLGLNLPH--------------------------PYPSPSMGEN-------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 282 ddvealnvsfpYGALpddfqRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYSNFDV 361
Cdd:cd16171 188 -----------FGSI-----RNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEG 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043871144 362 ATRVPLIFYVPGMTtspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAGLRVPP 427
Cdd:cd16171 252 SSHVPLLIMGPGIK------------------------AGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
46-426 |
3.76e-21 |
|
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: 96.34 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRpvlgcYGDKLVKS-PN-----IDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYD----FYS 115
Cdd:cd16160 3 NIVLFFADDMG-----YGDLASYGhPTqergpIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGgtrvFLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 116 YWRVHAGNYS-TMPQYFKENGYVTLSVGKvFHPGVSSNYSDDYPYSwsipPFHpsaekhendktcRGKDgklhanLVcpv 194
Cdd:cd16160 78 WDIGGLPKTEvTMAEALKEAGYTTGMVGK-WHLGINENNHSDGAHL----PSH------------HGFD------FV--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 195 nvtempeGT-LPdiqsteeaihLLNVMkttrqkfflAVGYHKPHIPLRYPQeflKLYPLENITLAPDPWVPKKLPSVAYN 273
Cdd:cd16160 132 -------GTnLP----------FTNSW---------ACDDTGRHVDFPDRS---ACFLYYNDTIVEQPIQHEHLTETLVG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 274 PWVDIRQrDDVEA---LNVSFPYGALP----DDFQ-RQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGW 345
Cdd:cd16160 183 DAKSFIE-DNQENpffLYFSFPQTHTPlfasKRFKgKSKRGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGP 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 346 SL---GEHGEWA-----KYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvSVPQGQSKEVVELVSLFPTL 417
Cdd:cd16160 262 HVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPG------------------------TIKPRVSHEVVSTMDIFPTF 317
|
....*....
gi 2043871144 418 AELAGLRVP 426
Cdd:cd16160 318 VDLAGGTLP 326
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
46-427 |
1.79e-20 |
|
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: 93.69 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRpvlgcYGD-------KLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWR 118
Cdd:cd16161 3 NFLLLFADDLG-----WGDlganwapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVGHNFLPTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 119 VhAG---NYSTMPQYFKENGYVTLSVGKvFHPGVSSNYsddypyswsippfHPSAekhendktcRGKDGKLHANLVCPVN 195
Cdd:cd16161 78 V-GGlplNETTLAEVLRQAGYATGMIGK-WHLGQREAY-------------LPNS---------RGFDYYFGIPFSHDSS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 196 VTEmpegtlpdiQSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPLRYPQEFlklyplenitlapdpwvpkklpsvayNPW 275
Cdd:cd16161 134 LAD---------RYAQFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRF--------------------------QSP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 276 VDIRQrddvealnvsfPYGalpddfqrqirqsyyAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHG-WSLG------ 348
Cdd:cd16161 179 TSGRG-----------PYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavg 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 349 -EHGEW--------AKYSNFDVATRVPLIFYVPGMttspvsqgarvfpyldpfsyigvsVPQG-QSKEVVELVSLFPTLA 418
Cdd:cd16161 233 pGTGDWqgnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANsTSAALVSTLDIFPTVV 288
|
....*....
gi 2043871144 419 ELAGLRVPP 427
Cdd:cd16161 289 ALAGASLPP 297
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
46-426 |
4.71e-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: 93.51 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRP-----DTTRLYDFYSYWRV 119
Cdd:cd16159 3 NIVLFMADDLGiGDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPirsgmASSHGMRVILFTAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 120 HAG---NYSTMPQYFKENGYVTLSVGKvFHPGVSSNYSDDYpyswsipPFHPSaeKH----------ENDKTCRGKDGKl 186
Cdd:cd16159 83 SGGlppNETTFAEVLKQQGYSTALIGK-WHLGLHCESRNDF-------CHHPL--NHgfdyfyglplTNLKDCGDGSNG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 187 hANLVCPVNVTEMPEGTLPdIQSTEEAIHLLNVMKTTRQKFFLAVGYhkpHIPLRYPQEFLKLYP------LENITLAPD 260
Cdd:cd16159 152 -EYDLSFDPLFPLLTAFVL-ITALTIFLLLYLGAVSKRFFVFLLILS---LLFISLFFLLLITNRyfncilMRNHEVVEQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 261 PWVPKKLPSVAYNPWVDI--RQRDDVEALNVSF-----PYGALPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSN 333
Cdd:cd16159 227 PMSLENLTQRLTKEAISFleRNKERPFLLVMSFlhvhtALFTSKKFKGRSKHGRYGDNVEEMDWSVGQILDALDELGLKD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 334 NTIVVFTADHGWSL------GEHGEW-------AKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldpfsyigvSVP 400
Cdd:cd16159 307 NTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPG------------------------VIP 362
|
410 420
....*....|....*....|....*....
gi 2043871144 401 QGqsKEVVELVS---LFPTLAELAGLRVP 426
Cdd:cd16159 363 PG--SVIDEPTSlmdIFPTVAALAGAPLP 389
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
46-426 |
2.11e-18 |
|
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: 88.27 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL-RPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTRLYDFYSYWRVHAG-- 122
Cdd:cd16158 3 NIVLLFADDLgYGDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVYPGVFYPGSRGGlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 123 -NYSTMPQYFKENGYVTLSVGKvFHPGVSSNYS--------DDY---PYSWSIPP------FHPsaekhenDKTCrgkDG 184
Cdd:cd16158 83 lNETTIAEVLKTVGYQTAMVGK-WHLGVGLNGTylpthqgfDHYlgiPYSHDQGPcqnltcFPP-------NIPC---FG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 185 KLHANLV-CPVNVTEMPEGTLPDIQSTEE-----AIHLLNVMKTTRQKFFLAVGYHKPHiplrYPQeflklyplenitla 258
Cdd:cd16158 152 GCDQGEVpCPLFYNESIVQQPVDLLTLEEryakfAKDFIADNAKEGKPFFLYYASHHTH----YPQ-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 259 pdpwvpkkLPSVAYNpwvdirqrddvealnvsfpygalpddfQRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVV 338
Cdd:cd16158 214 --------FAGQKFA---------------------------GRSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 339 FTADHGWSL------GEHG--EWAKYSNFDVATRVPLIFYVPGMttspvsqgarvfpyLDPfsyigvsvpqGQSKEVVEL 410
Cdd:cd16158 259 FTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPGR--------------IKP----------GVTHELAST 314
|
410
....*....|....*.
gi 2043871144 411 VSLFPTLAELAGLRVP 426
Cdd:cd16158 315 LDILPTIAKLAGAPLP 330
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
46-426 |
7.70e-17 |
|
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: 83.29 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLR-PVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRRPDTTrlyDFYSYwRVHAGNY 124
Cdd:cd16157 3 NIILMLMDDMGwGDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRN---GFYTT-NAHARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 ST--------------MPQYFKENGYVTLSVGKvFHPGVSsnysddypyswsiPPFHPSaeKHENDK-----TCRGK--D 183
Cdd:cd16157 79 YTpqnivggipdseilLPELLKKAGYRNKIVGK-WHLGHR-------------PQYHPL--KHGFDEwfgapNCHFGpyD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 184 GKLHANLvcPV-----------------------NVTEMpegtlpdiqSTEEAIHLLNVMKTTRQKFFLAVGYHKPHIPL 240
Cdd:cd16157 143 NKAYPNI--PVyrdwemigryyeefkidkktgesNLTQI---------YLQEALEFIEKQHDAQKPFFLYWAPDATHAPV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 241 RYPQEFLKlyplenitlapdpwvpkklpsvaynpwvdirqrddvealnvsfpygalpddfqRQIRQSYYAAVSYLDVQIG 320
Cdd:cd16157 212 YASKPFLG-----------------------------------------------------TSQRGLYGDAVMELDSSVG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 321 LLLSALDDAGLSNNTIVVFTADHGWSL-------GEHGEW--AKYSNFDVATRVPLIFYVPGmttspvsqgarvfpyldp 391
Cdd:cd16157 239 KILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPG------------------ 300
|
410 420 430
....*....|....*....|....*....|....*.
gi 2043871144 392 fsyigvSVPQGQ-SKEVVELVSLFPTLAELAGLRVP 426
Cdd:cd16157 301 ------HIKPGQvSHQLGSLMDLFTTSLALAGLPIP 330
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
46-461 |
1.74e-16 |
|
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: 81.24 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL----RPVLGcYGDKLVKSPNIDQLASQSMVFSNAYAqQAVCAPSRVSFLTGR---RPDTTRLYDfysywr 118
Cdd:cd16154 2 NILLIIADDQgldsSAQYS-LSSDLPVTPTLDSLANSGIVFDNLWA-TPACSPTRATILTGKygfRTGVLAVPD------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 119 VHAGNYSTMPQYFKEN----GYVTLSVGK---------VFHPGVSSNYS-------DDYpYSWsippfhpsaEKHENDKT 178
Cdd:cd16154 74 ELLLSEETLLQLLIKDattaGYSSAVIGKwhlggndnsPNNPGGIPYYAgilgggvQDY-YNW---------NLTNNGQT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 179 crgkdgklhanlvcpVNVTEMPEGtlpdiQSTEEAIHLLNvmKTTrQKFFLAVGYHKPHIPLRYPqeflklyP--LENIT 256
Cdd:cd16154 144 ---------------TNSTEYATT-----KLTNLAIDWID--QQT-KPWFLWLAYNAPHTPFHLP-------PaeLHSRS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 257 LAPDPwvpkklpsvaynpwVDIRQRDdvealnvsfpygalpddfqrqiRQSYYAAVSYLDVQIGLLLSALDDAGLsNNTI 336
Cdd:cd16154 194 LLGDS--------------ADIEANP----------------------RPYYLAAIEAMDTEIGRLLASIDEEER-ENTI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 337 VVFTADHG--------WSLGEHgewAKYSNFDVATRVPLIFYvpgmttspvsqgarvfpyldpfsyiGVSVPQGQSKE-- 406
Cdd:cd16154 237 IIFIGDNGtpgqvvdlPYTRNH---AKGSLYEGGINVPLIVS-------------------------GAGVERANEREsa 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2043871144 407 VVELVSLFPTLAELAGLRVPPACPEMSFgVALCTEGRSIVHYFNISKGEVGEGKE 461
Cdd:cd16154 289 LVNATDLYATIAELAGVDAAEIHDSVSF-KPLLSDVNASTRQYNYTEYESPTTTG 342
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
46-438 |
6.39e-16 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 80.85 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL-RPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVCAPSRVSFLTGRrPDTTRLYDFYSYWRvhaGNY 124
Cdd:COG1368 236 NVVVILLESFsDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGL-PPLPGGSPYKRPGQ---NNF 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 125 STMPQYFKENGYVTLsvgkVFHPGvssnysddYPYSWSIPPFHPSAekhendktcrGKDgklhaNLVCPVNVTEMPEGT- 203
Cdd:COG1368 312 PSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKNL----------GFD-----EFYDREDFDDPFDGGw 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 204 -LPDIQSTEEAIHLLNVMKttrQKFFLAV----GyhkpHIPLRYPQEFLKLYPLENITLapdpwvpkklpsvaynpwvdi 278
Cdd:COG1368 365 gVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL--------------------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 279 rqrddvealnvsfpygalpddfqrqirQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADH-GWSLGEHGEWAKYS 357
Cdd:COG1368 417 ---------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHgPRSPGKTDYENPLE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 358 NFdvatRVPLIFYVPGMTTSPVsqgarvfpyldpfsyigVSVPQGQskevvelVSLFPTLAELAGLRVPpacPEMSFGVA 437
Cdd:COG1368 470 RY----RVPLLIYSPGLKKPKV-----------------IDTVGSQ-------IDIAPTLLDLLGIDYP---SYYAFGRD 518
|
.
gi 2043871144 438 L 438
Cdd:COG1368 519 L 519
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
305-421 |
2.21e-15 |
|
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: 75.92 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 305 RQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGEWAKYS----NFDVATRVPLIFYVPGMTTspvs 380
Cdd:cd00016 141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPGVKK---- 216
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2043871144 381 qgarvfpyldpfsyigvsvpQGQSKEVVELVSLFPTLAELA 421
Cdd:cd00016 217 --------------------GGVKHELISQYDIAPTLADLL 237
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
46-422 |
2.55e-15 |
|
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: 76.57 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDL-RPVLGCYGDKLVKSPNIDQLASQSMVFSNAYAQQAVC--APSRVSFLTGRRPDTTRLYDFYSYwrvHAG 122
Cdd:cd16015 2 NVIVILLESFsDPYIDKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGgtANGEFEVLTGLPPLPLGSGSYTLY---KLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 123 NYSTMPQYFKENGYVTLSvgkvFHPGVSSNYSDD--YPY-----SWSIPPFhpsaekhENDKTCRGKDGklhanlvcpvn 195
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGGDASFYNRDsvYPNlgfdeFYDLEDF-------PDDEKETNGWG----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 196 vtempegtLPDIQSTEEAIHLLNvmKTTRQKFF---LAVGYHKPhiplrypqeflklYPLenitlaPDPWVPKKLPSVAY 272
Cdd:cd16015 137 --------VSDESLFDQALEELE--ELKKKPFFiflVTMSNHGP-------------YDL------PEEKKDEPLKVEED 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 273 NPWVDirqrddvealnvsfpygalpddfqrqirqSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGE 352
Cdd:cd16015 188 KTELE-----------------------------NYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYD 238
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 353 WAKYSNFDvATRVPLIFYVPGMTtspvsqgarvfpyldpfsyigvsvPQGQSKEVVELVSLFPTLAELAG 422
Cdd:cd16015 239 ETDEDPLD-LYRTPLLIYSPGLK------------------------KPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
304-389 |
2.98e-14 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 75.71 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 304 IRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHGE--WAKYSNF-DVATRVPLIFYVPGmttspvs 380
Cdd:COG3083 425 FKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFsRYQLQVPLVIHWPG------- 497
|
....*....
gi 2043871144 381 QGARVFPYL 389
Cdd:COG3083 498 TPPQVISKL 506
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
310-422 |
9.26e-07 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 50.66 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 310 AAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWS-LGEHGewakYSNFDVATRVPLIFYVPGmttspVSQGARVfpy 388
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA-----FKKGKKL--- 250
|
90 100 110
....*....|....*....|....*....|....
gi 2043871144 389 lDPFsyigvsvpqgqskevvELVSLFPTLAELAG 422
Cdd:cd16018 251 -GPF----------------RNVDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
296-370 |
5.63e-05 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 45.31 E-value: 5.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043871144 296 LPDDFQRQIRQSYYAAVSYLDVQIGLLLSALDDAGlsNNTIVVFTADHGWSLGEHGEW--AKYSNFDVATRVPLIFY 370
Cdd:cd16017 176 LQSCSKEELINAYDNSILYTDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIW 250
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
46-344 |
6.92e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.12 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 46 NVLFIIVDDLRPvlgcygDKL--VKSPNIDQLASQSMVFSNAYAQQ-AVCAPSRVSFLTGRRPDTTRLYdfysywrvhaG 122
Cdd:COG1524 25 KVVLILVDGLRA------DLLerAHAPNLAALAARGVYARPLTSVFpSTTAPAHTTLLTGLYPGEHGIV----------G 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 123 NYstmpQYFKENGYVTLSVGKVFHPGVSSNYsddypysWSIPPFHPSAEKHenDKTCR-------GKDGKLHANLVCPVN 195
Cdd:COG1524 89 NG----WYDPELGRVVNSLSWVEDGFGSNSL-------LPVPTIFERARAA--GLTTAavfwpsfEGSGLIDAARPYPYD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 196 vtempeGTLPDIQSTEEAIHLLNVMKTTRQKfflavgyHKPHIplrypqeflklyplenitlapdpwvpkklpSVAYNPW 275
Cdd:COG1524 156 ------GRKPLLGNPAADRWIAAAALELLRE-------GRPDL------------------------------LLVYLPD 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 276 VD-IRQRddvealnvsfpYGalPDDfqrqirQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHG 344
Cdd:COG1524 193 LDyAGHR-----------YG--PDS------PEYRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
319-438 |
4.25e-04 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 42.55 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 319 IGLLLSALDDAGLSNNTIVVFTADHGWS-LGEHGEwAKYSNfdvaTRVPLIFYVPGMTTSPVSQGarvfpylDPFSYIgv 397
Cdd:cd16024 180 IKRIYESLEEQSSNNPTLLVVCGDHGMTdAGNHGG-SSPGE----TSVPLLFISPKFSSKPSNAD-------GELSYY-- 245
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2043871144 398 svpqgqskEVVELVSLFPTLAELAGLRVppacPEMSFGVAL 438
Cdd:cd16024 246 --------ETVQQVDLAPTLALLLGLPI----PKNSVGVLI 274
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
308-399 |
6.35e-04 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 42.44 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 308 YYAAVSYLDVQIGLLLSALDDaglsnNTIVVFTADHG----WSLGEHgewakysnfdvaTR--VPLIFYVPGMTtsPVSQ 381
Cdd:cd16009 294 YAEALEEFDRRLPELLAKLKE-----DDLLIITADHGndptIGGTDH------------TReyVPLLVYGKGLK--GVNL 354
|
90
....*....|....*...
gi 2043871144 382 GARvfpylDPFSYIGVSV 399
Cdd:cd16009 355 GTR-----ETFADIGATI 367
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
310-344 |
4.56e-03 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 39.33 E-value: 4.56e-03
10 20 30
....*....|....*....|....*....|....*
gi 2043871144 310 AAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHG 344
Cdd:pfam01663 189 DALRRVDRAIGDLLEALDERGLFEDTNVIVVSDHG 223
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
308-399 |
5.35e-03 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 39.33 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 308 YYAAVSYLDVQIGLLLSALDDaglsnNTIVVFTADHG----WSLGEHgewakysnfdvaTR--VPLIFYVPGMTtsPVSQ 381
Cdd:PRK05362 301 YAAALEEFDARLPELLAALKE-----DDLLIITADHGndptWPGTDH------------TReyVPLLVYGPKFK--GGSL 361
|
90
....*....|....*...
gi 2043871144 382 GARvfpylDPFSYIGVSV 399
Cdd:PRK05362 362 GHR-----ETFADIGATI 374
|
|
| AP-SPAP |
cd16016 |
SPAP is a subclass of alkaline phosphatase (AP); Alkaline phosphatases are non-specific ... |
294-429 |
6.53e-03 |
|
SPAP is a subclass of alkaline phosphatase (AP); 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. Although SPAP is a subclass of alkaline phosphatase, SPAP has many differences from other APs: 1) the catalytic residue is a threonine instead of serine, 2) there is no binding pocket for the third metal ion, and 3) the arginine residue forming bidentate hydrogen bonding is deleted in SPAP. A lysine and an asparagine residue, recruited together for the first time into the active site, bind the substrate phosphoryl group in a manner not observed before in any other AP.
Pssm-ID: 293740 [Multi-domain] Cd Length: 457 Bit Score: 39.05 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043871144 294 GALPDDFQRQIRQSYYAAVS---YLDVQIGlllsalddaglsnntivVFTADHGWSLGEHGEWAKYsnfdvATRVPLIFY 370
Cdd:cd16016 359 GPEPTGIRERLRNGYNPKRSgdlIVVLKPG-----------------WIEGDGSGKGTTHGSPYDY-----DTHVPLLFY 416
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2043871144 371 VPGmttspvsqgarvfpyldpfsyigvsVPQGQSKEVVELVSLFPTLAELAGLRVPPAC 429
Cdd:cd16016 417 GWG-------------------------IKPGEIPRPVEITDIAPTLAALLGIQPPNGC 450
|
|
| OpgE |
COG2194 |
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall ... |
301-351 |
8.77e-03 |
|
Phosphoethanolamine transferase for periplasmic glucans OpgE, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441797 [Multi-domain] Cd Length: 537 Bit Score: 38.68 E-value: 8.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2043871144 301 QRQIRQSYYAAVSYLDVQIGLLLSALDDAGLSNNTIVVFTADHGWSLGEHG 351
Cdd:COG2194 407 REELVNAYDNTILYTDYVLSQVIDLLKAKQDRYDTAMLYVSDHGESLGENG 457
|
|
| |
