|
Name |
Accession |
Description |
Interval |
E-value |
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
5-450 |
8.93e-167 |
|
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: 476.68 E-value: 8.93e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGITsnHTDDSPYSWSFPPYHPSSEKYENTKTCRGP 84
Cdd:cd16030 61 RRPDTTGVYDNNSYFRKVAPDAVTLPQYFKENGYTTAGVGKIFHPGIP--DGDDDPASWDEPPNPPGPEKYPPGKLCPGK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 85 DGELHANLLCPVDVVDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSE 164
Cdd:cd16030 139 KGGKGGGGGPAWEAADVPDEAYPDGKVADEAIEQLRKLKDSDKPFFLAVGFYKPHLPFVAPKKYFDLYPLESIPL-PNPF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 165 VPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSD 244
Cdd:cd16030 218 DPIDLPEVAWNDLDDLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTIVVLWSD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 245 HGWALGEHGEWAKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd16030 298 HGWHLGEHGHWGKHTLFEEATRVPLIIRAPGVTK------------------------PGKVTDALVELVDIYPTLAELA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 325 GLQVPPrcpvpsfhvelCREGKNLLkhfrfrdleedPYL--PGNPRELIAYSQYPRPAdfpqwnsdkpslkdikIMGYSI 402
Cdd:cd16030 354 GLPAPP-----------CLEGKSLV-----------PLLknPSAKWKDAAFSQYPRPS----------------IMGYSI 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622970030 403 RTIDYRYTVWVgfnpdeflaNFSDIHAGELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16030 396 RTERYRYTEWV---------DFDKVGAEELYDHKNDPNEWKNLANDPE 434
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
5-448 |
3.42e-53 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 183.16 E-value: 3.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 5 RRPDTTRLYDFNSYWRVH-AGNFSTIPQYFKENGYVTMSVGKVFHpgitsnHTDDspyswsfppyhpssekyentktcrg 83
Cdd:COG3119 83 RYPHRTGVTDNGEGYNGGlPPDEPTLAELLKEAGYRTALFGKWHL------YLTD------------------------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 84 pdgELhanllcpvdvvdvpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENItlapds 163
Cdd:COG3119 132 ---LL-----------------------TDKAIDFLERQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDI------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 164 EVPDGLPPVAYNPwmdirqredvqalnisvpygpipvEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTS 243
Cdd:COG3119 180 PLPPNLAPRDLTE------------------------EELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 244 DHGWALGEHG-EWAKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAG 322
Cdd:COG3119 236 DNGPSLGEHGlRGGKGTLYEGGIRVPLIVRWPGKIK------------------------AGSVSDALVSLIDLLPTLLD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 323 LAGLQVPPRCpvpsfhvelcrEGKNLLKHFRFRDLEEDPYLpgnpreliaYSQYPRPAdfpqwnsdkpslkdikiMGYSI 402
Cdd:COG3119 292 LAGVPIPEDL-----------DGRSLLPLLTGEKAEWRDYL---------YWEYPRGG-----------------GNRAI 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622970030 403 RTIDYRYTVWVGFNPDEflanfsdihagELYFVDSDPLQDHNMYND 448
Cdd:COG3119 335 RTGRWKLIRYYDDDGPW-----------ELYDLKNDPGETNNLAAD 369
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
13-459 |
3.05e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 138.12 E-value: 3.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 13 YDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvFHPGitsnhTDDSPYSWSFPPYHPssekYENTKtcrgpdgelhanl 92
Cdd:cd16033 72 ENAGAYSRGLPPGVETFSEDLREAGYRNGYVGK-WHVG-----PEETPLDYGFDEYLP----VETTI------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 93 lcpvdvvdvpEGTLpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDSEVP-DGLPP 171
Cdd:cd16033 129 ----------EYFL-----ADRAIEMLEELAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDfEDKPY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 172 VAYNpwmdIRQREDVQALNIsvpygpipvEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGE 251
Cdd:cd16033 194 IYRR----ERKRWGVDTEDE---------EDWKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 252 HGEWAK-YSNFDVATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16033 261 HRLWDKgPFMYEETYRIPLIIKWPG------------------------VIAAGQVVDEFVSLLDLAPTILDLAGVDVPP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 331 RCpvpsfhvelcrEGKNLLkhfrfrdleedPYLPGNPRELIaysqypRPADFPQWNSDKPSLkdikiMGYSIRTIDYRYT 410
Cdd:cd16033 317 KV-----------DGRSLL-----------PLLRGEQPEDW------RDEVVTEYNGHEFYL-----PQRMVRTDRYKYV 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1622970030 411 vwvgFNPdeflanfSDIhaGELYFVDSDPLQDHNMYNDSQGGDLFQLLM 459
Cdd:cd16033 364 ----FNG-------FDI--DELYDLESDPYELNNLIDDPEYEEILREMR 399
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
28-444 |
2.40e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 126.91 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHpgITSNHTDDSPYSWSFPP-----------------YHPSSEKYENtktcrgpDGELHa 90
Cdd:cd16034 81 TIADVLKDAGYRTGYIGK-WH--LDGPERNDGRADDYTPPperrhgfdywkgyecnhDHNNPHYYDD-------DGKRI- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 91 nllcpvdvvdVPEGTLPDKQsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRY-PKEFQKLYPLENITLAPDseVPDGL 169
Cdd:cd16034 150 ----------YIKGYSPDAE-TDLAIEYLENQADKDKPFALVLSWNPPHDPYTTaPEEYLDMYDPKKLLLRPN--VPEDK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 170 PPVAynpwmdirqredvqalnisvpygpipvEFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL 249
Cdd:cd16034 217 KEEA---------------------------GLREDLRG-YYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDML 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 250 GEHGEWAKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16034 269 GSHGLMNKQVPYEESIRVPFIIRYPGK------------------------IKAGRVVDLLINTVDIMPTLLGLCGLPIP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 330 PrcpvpsfhvelCREGKNLLKHFrfrdLEEDPYLPGNpreliAYSQYPRPadFPQWNSDKPSLKDIkimgysIRTIDYRY 409
Cdd:cd16034 325 D-----------TVEGRDLSPLL----LGGKDDEPDS-----VLLQCFVP--FGGGSARDGGEWRG------VRTDRYTY 376
|
410 420 430
....*....|....*....|....*....|....*
gi 1622970030 410 TVWVGfnpDEFLanfsdihageLYFVDSDPLQDHN 444
Cdd:cd16034 377 VRDKN---GPWL----------LFDNEKDPYQLNN 398
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
112-350 |
1.85e-31 |
|
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: 123.83 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 112 TEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSEVPdgLPPVAyNPWMDIRqreDVQALni 191
Cdd:cd16155 108 ADAAIEFLEEYKDGDKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPL-PENFLP--QHPFD-NGEGTVR---DEQLA-- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 192 svPYGPIPVEFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVATHVPLMF 271
Cdd:cd16155 179 --PFPRTPEAVRQHLAE-YYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGLMGKQNLYEHSMRVPLII 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970030 272 YVPGrtasLPeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLK 350
Cdd:cd16155 256 SGPG----IP---------------------KGKRRDALVYLQDVFPTLCELAGIEIPESV-----------EGKSLLP 298
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
100-439 |
9.26e-31 |
|
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: 121.11 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 100 DVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdsevpdglppvaynpwmd 179
Cdd:cd16037 104 DQRHGFRYDRDVTEAAVDWLREEAADDKPWFLFVGFVAPHFPLIAPQEFYDLY--------------------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 180 irqredvqalnisvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYS 259
Cdd:cd16037 157 -----------------------VRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLWGKST 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 260 NFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPvpsfhv 339
Cdd:cd16037 214 MYEESVRVPMIISGPGI-------------------------PAGKRVKTPVSLVDLAPTILEAAGAPPPPDLD------ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 340 elcreGKNLLkhfrfrDLEEDPYlpgnPRELIAYSQYprpadfpqwnsdkpSLKDIKIMGYSIRTIDYRYTVWVGFNPde 419
Cdd:cd16037 263 -----GRSLL------PLAEGPD----DPDRVVFSEY--------------HAHGSPSGAFMLRKGRWKYIYYVGYPP-- 311
|
330 340
....*....|....*....|
gi 1622970030 420 flanfsdihagELYFVDSDP 439
Cdd:cd16037 312 -----------QLFDLENDP 320
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
28-330 |
1.50e-30 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 123.24 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKV----------FHpgitsNHTDDSPYSWSFPPYHPSseKYENTKTCR--------GPDGEL- 88
Cdd:PRK13759 87 TLPQEFRDAGYYTQCIGKMhvfpqrnllgFH-----NVLLHDGYLHSGRNEDKS--QFDFVSDYLawlrekapGKDPDLt 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 89 ------HANLLCPVDVvdvPEGTLPDKQSTEQAIQLLEKmKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapD 162
Cdd:PRK13759 160 digwdcNSWVARPWDL---EERLHPTNWVGSESIEFLRR-RDPTKPFFLKMSFARPHSPYDPPKRYFDMYK--------D 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 163 SEVPDglPPVAynPWmDIRQREDVQALNISVPYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFT 242
Cdd:PRK13759 228 ADIPD--PHIG--DW-EYAEDQDPEGGSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 243 SDHGWALGEHGEWAKYSNFDVATHVPLMFYVPGRTASLPEageklfpyldpfdsaselmepGRQSMDLVELVSLFPTLAG 322
Cdd:PRK13759 303 SDHGDMLGDHYLFRKGYPYEGSAHIPFIIYDPGGLLAGNR---------------------GTVIDQVVELRDIMPTLLD 361
|
....*...
gi 1622970030 323 LAGLQVPP 330
Cdd:PRK13759 362 LAGGTIPD 369
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
128-376 |
8.26e-29 |
|
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: 115.75 E-value: 8.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 128 PFFLAVGYHKPHIPFRYPKEFQKLYplenitlapdsevpdglppvaynpwmdirqredvqalnisvpygpipvefQRKIR 207
Cdd:cd16032 134 PFFLTVSFTHPHDPYVIPQEYWDLY--------------------------------------------------VRRAR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 208 QSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVATHVPLMFYVPGRTAslpeagekl 287
Cdd:cd16032 164 RAYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSFFEGSARVPLIISAPGRFA--------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 288 fpyldpfdsaselmePGRQSmDLVELVSLFPTLAGLAGLQVPPRCPVPsfhvelcrEGKNLLKHFRFRDleedpylPGNP 367
Cdd:cd16032 235 ---------------PRRVA-EPVSLVDLLPTLVDLAGGGTAPHVPPL--------DGRSLLPLLEGGD-------SGGE 283
|
....*....
gi 1622970030 368 REliAYSQY 376
Cdd:cd16032 284 DE--VISEY 290
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
28-458 |
6.48e-28 |
|
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: 114.93 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPSSEKYENtKTCRGPDGEL-HANLLCpvdvvdvpegtl 106
Cdd:cd16031 83 TYPKLLRKAGYQTAFIGK-WHLGSGGDLPPPGFDYWVSFPGQGSYYDPEF-IENGKRVGQKgYVTDII------------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 107 pdkqsTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLaPDSEVPD---GLPPVAYNPWMDIRQR 183
Cdd:cd16031 149 -----TDKALDFLKERDKD-KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPE-PETFDDDdyaGRPEWAREQRNRIRGV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 184 EDVQALNisvpygpiPVEFQRKIRQsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGeWA-KYSNFD 262
Cdd:cd16031 222 LDGRFDT--------PEKYQRYMKD-YLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHG-LFdKRLMYE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 263 VATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelc 342
Cdd:cd16031 292 ESIRVPLIIRDPRLI------------------------KAGTVVDALVLNIDFAPTILDLAGVPIPEDM---------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 343 rEGKNLLKHFRFRDleedpylPGNPRE--LIAYSQYPRPADFPQWnsdkpslkdikimgYSIRTIDYRYTVWVGFNPDEf 420
Cdd:cd16031 338 -QGRSLLPLLEGEK-------PVDWRKefYYEYYEEPNFHNVPTH--------------EGVRTERYKYIYYYGVWDEE- 394
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622970030 421 lanfsdihagELYFVDSDPLQDHNMYNDSQGGDLFQLL 458
Cdd:cd16031 395 ----------ELYDLKKDPLELNNLANDPEYAEVLKEL 422
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
5-329 |
8.29e-27 |
|
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: 107.91 E-value: 8.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgitsNHtddspyswsfppyhpssekyentktcrgp 84
Cdd:cd16022 60 RYPHRHGVRGNVGNGGGLPPDEPTLAELLKEAGYRTALIGK--------WH----------------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 85 dgelhanllcpvdvvdvpegtlpdkqstEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYpkefqklyplenitlapdse 164
Cdd:cd16022 103 ----------------------------DEAIDFIERRDKDK-PFFLYVSFNAPHPPFAY-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 165 vpdglppvaynpwmdirqredvqalnisvpygpipvefqrkirqsyFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSD 244
Cdd:cd16022 134 ----------------------------------------------YAMVSAIDDQIGRILDALEELGLLDNTLIVFTSD 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 245 HGWALGEHGE-WAKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGL 323
Cdd:cd16022 168 HGDMLGDHGLrGKKGSLYEGGIRVPFIVRWPGK------------------------IPAGQVSDALVSLLDLLPTLLDL 223
|
....*.
gi 1622970030 324 AGLQVP 329
Cdd:cd16022 224 AGIEPP 229
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
28-330 |
8.52e-27 |
|
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: 111.06 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKVFHPGitsnhtdDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANllcpvdvvdvpegtlP 107
Cdd:cd16027 82 TLPELLREAGYYTGLIGKTHYNP-------DAVFPFDDEMRGPDDGGRNAWDYASNAADFLNRA---------------K 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 108 DKQsteqaiqllekmktsasPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDseVPDgLPPVaynpwmdirqREDVQ 187
Cdd:cd16027 140 KGQ-----------------PFFLWFGFHDPHRPYPPGDGEEPGYDPEKVKVPPY--LPD-TPEV----------REDLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 188 AlnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGehgeWAKYSNFDVATHV 267
Cdd:cd16027 190 D---------------------YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP----RAKGTLYDSGLRV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970030 268 PLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16027 245 PLIVRWPGKI------------------------KPGSVSDALVSFIDLAPTLLDLAGIEPPE 283
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
15-331 |
1.05e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 108.40 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 15 FNSYWRVHAG----NFSTIPQYFKENGYVTMSVGkvfhpgitsnhtdDSPYSWSFPPYHPSSEKYENTktcRGPDGElha 90
Cdd:cd16148 61 YPFYHGVWGGplepDDPTLAEILRKAGYYTAAVS-------------SNPHLFGGPGFDRGFDTFEDF---RGQEGD--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 91 nllcpvdvvDVPEGTLPDKQSTEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYpkefqklyplenitlapdsevpdglp 170
Cdd:cd16148 122 ---------PGEEGDERAERVTDRALEWLDRNADD-DPFFLFLHYFDPHEPYLY-------------------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 171 pvaynpwmdirqreDvqalnisvpygpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALG 250
Cdd:cd16148 166 --------------D--------------------------AEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 251 EHGEWAK-YSNF-DVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQV 328
Cdd:cd16148 206 EHGLYWGhGSNLyDEQLHVPLIIRWPGK-------------------------EPGKRVDALVSHIDIAPTLLDLLGVEP 260
|
...
gi 1622970030 329 PPR 331
Cdd:cd16148 261 PDY 263
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
105-450 |
1.43e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 111.17 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 105 TLPDKQSTEQAIQLLEKMKTSAsPFFLAVGYHKPHIPFRYPKEFQKLYPLEnitLAPDsEVPDGLPpvAYNPWMDIRQRE 184
Cdd:cd16150 111 CDSDEACVRTAIDWLRNRRPDK-PFCLYLPLIFPHPPYGVEEPWFSMIDRE---KLPP-RRPPGLR--AKGKPSMLEGIE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 185 DvQALNisvpygPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSN-F-D 262
Cdd:cd16150 184 K-QGLD------RWSEERWRELRATYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVEKWPNtFeD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 263 VATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVPPrcpvPSFhvelc 342
Cdd:cd16150 257 CLTRVPLIIKPPGGP-------------------------AGGVSDALVELVDIPPTLLDLAGIPLSH----THF----- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 343 reGKNLLKHFRFRDLEEDPY-------LPGNPReliAYSQYPRPADFPQWNSDKPSLKDIKIMGYSIRTIDYRYtVWVGF 415
Cdd:cd16150 303 --GRSLLPVLAGETEEHRDAvfseggrLHGEEQ---AMEGGHGPYDLKWPRLLQQEEPPEHTKAVMIRTRRYKY-VYRLY 376
|
330 340 350
....*....|....*....|....*....|....*
gi 1622970030 416 NPDeflanfsdihagELYFVDSDPLQDHNMYNDSQ 450
Cdd:cd16150 377 EPD------------ELYDLEADPLELHNLIGDPA 399
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
128-385 |
4.55e-23 |
|
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: 101.18 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 128 PFFLAVGYHKPHIPFRYPKEFQKLYPLENITL---APDSEVPDGLPPVaYNPWMDIRQREDVQALNIsvPYGPIPVEFQR 204
Cdd:cd16028 158 PWFLHLSYIRPHPPFVAPAPYHALYDPADVPPpirAESLAAEAAQHPL-LAAFLERIESLSFSPGAA--NAADLDDEEVA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 205 KIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDVATHVPLMFYVPGRTAslpeag 284
Cdd:cd16028 235 QMRATYLGLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLWGKDGFFDQAYRVPLIVRDPRREA------ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 285 eklfpyldpfDSASelmepGRQSMDLVELVSLFPTLAGLAGLQVPPRCpvpsfhvelcrEGKNLLKHfrfrdLEEDPylP 364
Cdd:cd16028 309 ----------DATR-----GQVVDAFTESVDVMPTILDWLGGEIPHQC-----------DGRSLLPL-----LAGAQ--P 355
|
250 260
....*....|....*....|.
gi 1622970030 365 GNPRELIAYSQYPRPADFPQW 385
Cdd:cd16028 356 SDWRDAVHYEYDFRDVSTRRP 376
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
28-329 |
3.08e-22 |
|
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: 98.02 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHPGITSNH--TD---DS----PYS---WSFPPYHPSSEKYEntktcrgpdgelhANLLCP 95
Cdd:cd16026 87 TIAEVLKKAGYRTALVGK-WHLGHQPEFlpTRhgfDEyfgiPYSndmWPFPLYRNDPPGPL-------------PPLMEN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 96 VDVVDVPegtlPD-----KQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKlyplenitlapDSEvpDGLp 170
Cdd:cd16026 153 EEVIEQP----ADqssltQRYTDEAVDFIERNKDQ--PFFLYLAHTMPHVPLFASEKFKG-----------RSG--AGL- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 171 pvaynpwmdirqredvqalnisvpYGpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALG 250
Cdd:cd16026 213 ------------------------YG---------------DVVEELDWSVGRILDALKELGLEENTLVIFTSDNGPWLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 251 EHGEW--------AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAG 322
Cdd:cd16026 254 YGGHGgsagplrgGKGTTWEGGVRVPFIAWWPGV------------------------IPAGTVSDELASTMDLLPTLAA 309
|
....*..
gi 1622970030 323 LAGLQVP 329
Cdd:cd16026 310 LAGAPLP 316
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
28-444 |
8.52e-22 |
|
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: 96.85 E-value: 8.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHPGitsnhtDDSPY----------------SWSFPPYHPSSEKYENTKTCRGpdgelhan 91
Cdd:cd16146 82 TLAEVFKDAGYRTGIFGK-WHLG------DNYPYrpqdrgfdevlghgggGIGQYPDYWGNDYFDDTYYHNG-------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 92 llcpvdVVDVPEGTLPDKQsTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapDSEVPDGlpp 171
Cdd:cd16146 147 ------KFVKTEGYCTDVF-FDEAIDFIEENKDK--PFFAYLATNAPHGPLQVPDKYLDPYK--------DMGLDDK--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 172 vaynpwmdirqredvqalnisvpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGE 251
Cdd:cd16146 207 -----------------------------------LAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAGGV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 252 HGEW------AKYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAG 325
Cdd:cd16146 252 PKRFnagmrgKKGSVYEGGHRVPFFIRWPGKIL------------------------AGKDVDTLTAHIDLLPTLLDLCG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 326 LQVPPrcpvpsfHVELcrEGKNLLKhfrfrdLEEDPYLPGNPRELIAYSQYPRPADFPQWNSdkpslkdikimgySIRTI 405
Cdd:cd16146 308 VKLPE-------GIKL--DGRSLLP------LLKGESDPWPERTLFTHSGRWPPPPKKKRNA-------------AVRTG 359
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622970030 406 DYRYTVWVGFNPdeflanfsdihagELYFVDSDPLQDHN 444
Cdd:cd16146 360 RWRLVSPKGFQP-------------ELYDIENDPGEEND 385
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
2-330 |
2.82e-21 |
|
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: 95.69 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 2 PLRRRPDTTRLYDFNSYWRVHAGNFsTIPQYFKENGYVTMSVGKvFHPGITSNHT--------DDSPYSWSFPPYHPSSE 73
Cdd:cd16144 73 GRRGPPDNTKLIPPPSTTRLPLEEV-TIAEALKDAGYATAHFGK-WHLGGEGGYGpedqgfdvNIGGTGNGGPPSYYFPP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 74 KYENTKTCRGPDGElhanllcpvdvvdvpegTLPDKqSTEQAIQLLEKmkTSASPFFLAVGYHKPHIPFRYPKEFQKLYP 153
Cdd:cd16144 151 GKPNPDLEDGPEGE-----------------YLTDR-LTDEAIDFIEQ--NKDKPFFLYLSHYAVHTPIQARPELIEKYE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 154 lenitlapdsEVPDGLPPVAYNPwmdirqredvqalnisvpygpipvefqrkirqSYFASVSYLDTQVGRLLSALDDLQL 233
Cdd:cd16144 211 ----------KKKKGLRKGQKNP--------------------------------VYAAMIESLDESVGRILDALEELGL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 234 ANSTIVAFTSDHGwALGEHGEWA---------KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePG 304
Cdd:cd16144 249 ADNTLVIFTSDNG-GLSTRGGPPtsnaplrggKGSLYEGGIRVPLIVRWPGVIK------------------------PG 303
|
330 340
....*....|....*....|....*.
gi 1622970030 305 RQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16144 304 SVSDVPVIGTDLYPTFLELAGGPLPP 329
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
5-328 |
7.96e-21 |
|
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: 92.05 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 5 RRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKvfhpgitsnhtddspyswsfppyhpssEKYENtktcrgp 84
Cdd:cd16153 71 RYPHRTGVYGFEAAHPALDHGLPTFPEVLKKAGYQTASFGK---------------------------SHLEA------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 85 dgelhanllcPVDVVDVPEgtlpdkQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFqklyplenitlapdse 164
Cdd:cd16153 117 ----------FQRYLKNAN------QSYKSFWGKIAKGADSDKPFFVRLSFLQPHTPVLPPKEF---------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 165 vpdglppvaynpwmdiRQREDvqalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLAN---STIVAF 241
Cdd:cd16153 165 ----------------RDRFD------------------------YYAFCAYGDAQVGRAVEAFKAYSLKQdrdYTIVYV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 242 TSDHGWALGEHGEWAKYSNFDVATHVPLMFYVPGRtaslpeageKLFPyldpfdsaselmePGRQSMDLVELVSLFPTLA 321
Cdd:cd16153 205 TGDHGWHLGEQGILAKFTFWPQSHRVPLIVVSSDK---------LKAP-------------AGKVRHDFVEFVDLAPTLL 262
|
....*..
gi 1622970030 322 GLAGLQV 328
Cdd:cd16153 263 AAAGVDV 269
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-326 |
3.24e-19 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 87.86 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 23 AGNFSTIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGpdgelhanlLCPVDVVDvp 102
Cdd:pfam00884 76 PRTEPSLPDLLKRAGYNTGAIGK-WHLGWYNNQSPCNLGFDKFFGRNTGSDLYADPPDVPY---------NCSGGGVS-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 103 egtlpDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevpdglppvaynpwmdirq 182
Cdd:pfam00884 144 -----DEALLDEALEFLDN---NDKPFFLVLHTLGSHGPPYYPDRYPEKYA----------------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 183 redvqalnISVPYGPipveFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFD 262
Cdd:pfam00884 187 --------TFKPSSC----SEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHGGKYD 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622970030 263 VA----THVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGL 326
Cdd:pfam00884 255 NApeggYRVPLLIWSPGGKA------------------------KGQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
210-337 |
3.64e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 86.91 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 210 YFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAK------YSNFDVATHVPLMFYVPGRTaslpea 283
Cdd:cd16149 144 YFAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIWGKgngtfpLNMYDNSVKVPFIIRWPGVV------ 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970030 284 geklfpyldpfdsaselmEPGRQSMDLVELVSLFPTLAGLAGLQVP--PRCPVPSF 337
Cdd:cd16149 218 ------------------PAGRVVDSLVSAYDFFPTLLELAGVDPPadPRLPGRSF 255
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
108-326 |
7.78e-18 |
|
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: 83.80 E-value: 7.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 108 DKQSTEQAIQLLEKMKTSAS---PFFLAVGYHKPHipfrypkefqklyplenitlapdsevpdglppvaynpwmdirqre 184
Cdd:cd16035 116 DPGIAAQAVEWLRERGAKNAdgkPWFLVVSLVNPH--------------------------------------------- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 185 DVQalnisvpYGPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSN-FDV 263
Cdd:cd16035 151 DIM-------FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGLRGKGFNaYEE 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970030 264 ATHVPLMFYVPGrtaslpeagekLFPyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGL 326
Cdd:cd16035 224 ALHVPLIISHPD-----------LFG-------------TGQTTDALTSHIDLLPTLLGLAGV 262
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
25-362 |
2.51e-17 |
|
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: 83.97 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 25 NFSTIPQYFKENGYVTMSVGK-------VFHPGITSNHTDdSPYSWSFPPYHPSSEKYENTKTCRGPDgELHANllcpvd 97
Cdd:cd16156 77 NVKTIGQRLSDNGIHTAYIGKwhldggdYFGNGICPQGWD-PDYWYDMRNYLDELTEEERRKSRRGLT-SLEAE------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 98 vvDVPEGTLPDKQSTEQAIQLLEKMKTSasPFFLAVGYHKPHIPFRYPKEFQKLYplenitlaPDSEVPDGlpPVAYN-- 175
Cdd:cd16156 149 --GIKEEFTYGHRCTNRALDFIEKHKDE--DFFLVVSYDEPHHPFLCPKPYASMY--------KDFEFPKG--ENAYDdl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 176 ---P-----WMDIRQREDVQALNISVPYgpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLqLANSTIVaFTSDHGW 247
Cdd:cd16156 215 enkPlhqrlWAGAKPHEDGDKGTIKHPL--------------YFGCNSFVDYEIGRVLDAADEI-AEDAWVI-YTSDHGD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 248 ALGEHGEWAK-YSNFDVATHVPLMFYVPGrtaslpeaGEKLFPYLD-PfdsaselmepgrqsmdlVELVSLFPTLAGLAG 325
Cdd:cd16156 279 MLGAHKLWAKgPAVYDEITNIPLIIRGKG--------GEKAGTVTDtP-----------------VSHIDLAPTILDYAG 333
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622970030 326 LQVPPRCP----VPSFHVELCREGKNLLKHFRFRDLEEDPY 362
Cdd:cd16156 334 IPQPKVLEgesiLATIEDPEIPENRGVFVEFGRYEVDHDGF 374
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-331 |
7.40e-17 |
|
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: 82.26 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKVfhpGITSNHTDDSPYS----------------WSFPPYhpsseKYENTKtcRGPDGELHAN 91
Cdd:cd16145 85 TLAEVLKKAGYATAAFGKW---GLGGPGTPGHPTKqgfdyfygyldqvhahNYYPEY-----LWRNGE--KVPLPNNVIP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 92 LLCPVDVVDVPEGTLPDKQSTEQAIQLLEKMKtsASPFFLAVGYHKPHIPFRYPKefqklyplenitLAPDSEVPDGLPP 171
Cdd:cd16145 155 PLDEGNNAGGGGGTYSHDLFTDEALDFIRENK--DKPFFLYLAYTLPHAPLQVPD------------DGPYKYKPKDPGI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 172 VAYNPWMDIRQRedvqalnisvpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGwALGE 251
Cdd:cd16145 221 YAYLPWPQPEKA--------------------------YAAMVTRLDRDVGRILALLKELGIDENTLVVFTSDNG-PHSE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 252 HGEWAKYSNFDVA--------------THVPLMFYVPGRTaslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLF 317
Cdd:cd16145 274 GGSEHDPDFFDSNgplrgykrslyeggIRVPFIARWPGKI------------------------PAGSVSDHPSAFWDFM 329
|
330
....*....|....
gi 1622970030 318 PTLAGLAGLQVPPR 331
Cdd:cd16145 330 PTLADLAGAEPPED 343
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
27-362 |
8.73e-17 |
|
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: 81.83 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 27 STIPQYFKENGYVTMSVGKVFHPGITSNHTDDSP--YSWSFPPYHPSseKYENTKTCRGPDGELHANllCPV----DVVd 100
Cdd:cd16147 85 STLPVWLQEAGYRTAYAGKYLNGYGVPGGVSYVPpgWDEWDGLVGNS--TYYNYTLSNGGNGKHGVS--YPGdyltDVI- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 101 vpegtlpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPleNITLAP-----DSEVPDG------L 169
Cdd:cd16147 160 -----------ANKALDFLRRAAADDKPFFLVVAPPAPHGPFTPAPRYANLFP--NVTAPPrpppnNPDVSDKphwlrrL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 170 PPvaynPWMDIRQREDvqalnisvpygpipvEFQRKIRQSyFASVsylDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL 249
Cdd:cd16147 227 PP----LNPTQIAYID---------------ELYRKRLRT-LQSV---DDLVERLVNTLEATGQLDNTYIIYTSDNGYHL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 250 GEHG-EWAKYSNFDVATHVPLMFYVPGrtasLPeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQV 328
Cdd:cd16147 284 GQHRlPPGKRTPYEEDIRVPLLVRGPG----IP---------------------AGVTVDQLVSNIDLAPTILDLAGAPP 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622970030 329 PP--------RCPVPSFH-VELCREGKNLLKHF---RFR---DLEEDPY 362
Cdd:cd16147 339 PSdmdgrscgDSNNNTYKcVRTVDDTYNLLYFEwctGFRelyDLTTDPY 387
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
189-330 |
1.69e-16 |
|
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: 80.66 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 189 LNISVPYgPIPVEFQ-----RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYSNFDV 263
Cdd:cd16171 173 LNLPHPY-PSPSMGEnfgsiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRQFYKMSMYEG 251
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622970030 264 ATHVPLMFYVPGrtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16171 252 SSHVPLLIMGPG-------------------------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQ 293
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-330 |
5.32e-16 |
|
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: 79.11 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvfhpgitsNHTDDSPYSWsfppyhPssekyentkTCRGPDgELHANLLcpvdvvdvpegTLP 107
Cdd:cd16142 87 TLAELLKDAGYATAQFGK--------WHLGDEDGRL------P---------TDHGFD-EFYGNLY-----------HTI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 108 DKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevpdglppvAYNPWMDirqredvq 187
Cdd:cd16142 132 DEEIVDKAIDFIKRNAKADKPFFLYVNFTKMHFPTLPSPEFEGKSS-------------------GKGKYAD-------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 188 alnisvpygpipvefqrkirqsyfaSVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG-----WALGEHGEW--AKYSN 260
Cdd:cd16142 185 -------------------------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFrgEKGTT 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 261 FDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16142 240 WEGGVRVPAIVRWPGK------------------------IKPGRVSNEIVSHLDWFPTLAALAGAPDPK 285
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
25-334 |
4.52e-15 |
|
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: 76.43 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 25 NFSTIPQYFKENGYVTMSVGKvFHPGItsnhtddspYSWSFPP----------YHPSSEKYENTKTCRGPDgelhanllC 94
Cdd:cd16029 82 NETLLPQYLKELGYATHLVGK-WHLGF---------YTWEYTPtnrgfdsfygYYGGAEDYYTHTSGGAND--------Y 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 95 PVDVVDVPEGTLPDKQS-------TEQAIQLLEKMKTSaSPFFLAVGYHKPHIPFRYPKEFQKLYPlenitlapdsevpd 167
Cdd:cd16029 144 GNDDLRDNEEPAWDYNGtystdlfTDRAVDIIENHDPS-KPLFLYLAFQAVHAPLQVPPEYADPYE-------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 168 glppvaynpwmdirqredVQALNIsvpygpipvefQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGw 247
Cdd:cd16029 209 ------------------DKFAHI-----------KDEDRRTYAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 248 ALGEHGEWA--------KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmEPGRQSMDLVELVSLFPT 319
Cdd:cd16029 259 GPTGGGDGGsnyplrggKNTLWEGGVRVPAFVWSPLLPP-----------------------KRGTVSDGLMHVTDWLPT 315
|
330
....*....|....*
gi 1622970030 320 LAGLAGLQVPPRCPV 334
Cdd:cd16029 316 LLSLAGGDPDDLPPL 330
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
192-444 |
9.90e-15 |
|
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: 75.33 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 192 SVPYGPIPVEFQRkiRQSYF-ASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEW-------AKYSNFDV 263
Cdd:cd16151 190 SPDWDPDDKRKKD--DPEYFpDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTngrevrgGKGKTTDA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 264 ATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVpsfhvelcr 343
Cdd:cd16151 268 GTHVPLIVNWPG------------------------LIPAGGVSDDLVDFSDFLPTLAELAGAPLPEDYPL--------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 344 EGKNLLkhfrfrdleedPYL---PGNPRELIAYsqyprpadfpqWNSDKPSLKDIKimgYSIRTIDYRYtvwvgfnpdef 420
Cdd:cd16151 315 DGRSFA-----------PQLlgkTGSPRREWIY-----------WYYRNPHKKFGS---RFVRTKRYKL----------- 358
|
250 260
....*....|....*....|....
gi 1622970030 421 lanFSDihaGELYFVDSDPLQDHN 444
Cdd:cd16151 359 ---YAD---GRFFDLREDPLEKNP 376
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
108-278 |
5.42e-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: 74.17 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 108 DKQSTEQAIQLLEKmKTSASPFFLAVGYHKPH---IPFRYPKEFQKLYPLENITLAPDSEVPdglppvaynpwmdirqre 184
Cdd:COG3083 363 DRQITAQWLQWLDQ-RDSDRPWFSYLFLDAPHaysFPADYPKPFQPSEDCNYLALDNESDPT------------------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 185 dvqalnisvpygpipvefqrKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGE--WAKYSNF- 261
Cdd:COG3083 424 --------------------PFKNRYRNAVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEEFNENGQnyWGHNSNFs 483
|
170
....*....|....*..
gi 1622970030 262 DVATHVPLMFYVPGRTA 278
Cdd:COG3083 484 RYQLQVPLVIHWPGTPP 500
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
28-329 |
6.84e-13 |
|
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: 69.92 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDgelHANLLCPVDVVDvpegTLp 107
Cdd:cd16143 87 TLAKMLKQAGYRTAMVGK-WHLGLDWKKKDGKKAATGTGKDVDYSKPIKGGPLDHGFD---YYFGIPASEVLP----TL- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 108 dkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLyplenitlapdSEVpdGlppvaynpwmdirqredvq 187
Cdd:cd16143 158 ----TDKAVEFIDQHAKKDKPFFLYFALPAPHTPIVPSPEFQGK-----------SGA--G------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 188 alnisvPYGpipvEFqrkIRQsyfasvsyLDTQVGRLLSALDDLQLANSTIVAFTSDHG-------WALGEHGEWA---- 256
Cdd:cd16143 202 ------PYG----DF---VYE--------LDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgpl 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622970030 257 ---KYSNFDVATHVPLMFYVPGRTAslpeageklfpyldpfdsaselmePGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16143 261 rgmKADIYEGGHRVPFIVRWPGKIP------------------------AGSVSDQLVSLTDLFATLAAIVGQKLP 312
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
210-330 |
4.64e-12 |
|
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: 67.25 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 210 YFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHgwalGEH-----GEWaKYSNFDVATHVPLMFYVPGrtaslpeag 284
Cdd:cd16152 177 YLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDH----GCHfrtrnAEY-KRSCHESSIRVPLVIYGPG--------- 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622970030 285 eklfpyldpFDSaselmepGRQSMDLVELVSLFPTLAGLAGLQVPP 330
Cdd:cd16152 243 ---------FNG-------GGRVEELVSLIDLPPTLLDAAGIDVPE 272
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
25-330 |
5.82e-11 |
|
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: 64.03 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 25 NFSTIPQYFKENGYVTMSVGKvFHPGITSNhtddspyswsfppYHPSSekyentktcRGPDGELHANLLCPVdvvdvpeg 104
Cdd:cd16161 84 NETTLAEVLRQAGYATGMIGK-WHLGQREA-------------YLPNS---------RGFDYYFGIPFSHDS-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 105 TLPDKQStEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQklyplenitlAPDSevpdglppvaynpwmdirqre 184
Cdd:cd16161 133 SLADRYA-QFATDFIQRASAKDRPFFLYAALAHVHVPLANLPRFQ----------SPTS--------------------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 185 dvqalnISVPYGpipvefqrkirqsyfASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG-WALG-------EHGEW- 255
Cdd:cd16161 181 ------GRGPYG---------------DALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpWEVKcelavgpGTGDWq 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 256 -------AKYSNFDVATHVPLMFYVPGRtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQV 328
Cdd:cd16161 240 gnlggsvAKASTWEGGHREPAIVYWPGR------------------------IPANSTSAALVSTLDIFPTVVALAGASL 295
|
..
gi 1622970030 329 PP 330
Cdd:cd16161 296 PP 297
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
207-324 |
5.87e-11 |
|
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: 62.44 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 207 RQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEHGEWAKYS----NFDVATHVPLMFYVPGRTAslpe 282
Cdd:cd00016 141 TPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDKGHGGDPKADgkadKSHTGMRVPFIAYGPGVKK---- 216
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622970030 283 ageklfpyldpfdsaselmepGRQSMDLVELVSLFPTLAGLA 324
Cdd:cd00016 217 ---------------------GGVKHELISQYDIAPTLADLL 237
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
28-329 |
1.01e-10 |
|
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: 63.23 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvfhpgitsnhtddspysW--SFPPYHpSSEKYentktcrgpdgelhanllcpvdvvdvpegt 105
Cdd:cd16025 90 TIAEVLKDAGYHTYMSGK-----------------WhlGPDDYY-STDDL------------------------------ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 106 lpdkqsTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEF----------------------QK---LYPlENITLA 160
Cdd:cd16025 122 ------TDKAIEYIDEQKAPDKPFFLYLAFGAPHAPLQAPKEWidkykgkydagwdalreerlerQKelgLIP-ADTKLT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 161 PDsevPDGLPPvaynpWMDIRQRE-DVQALNISVpygpipvefqrkirqsYFASVSYLDTQVGRLLSALDDLQLANSTIV 239
Cdd:cd16025 195 PR---PPGVPA-----WDSLSPEEkKLEARRMEV----------------YAAMVEHMDQQIGRLIDYLKELGELDNTLI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 240 AFTSDHGwALGEHGeWAKYSN-----FDVATH-----VPLMfyvpgrtASLPEAGEKlfpyldpfdsaselmePGRQSMD 309
Cdd:cd16025 251 IFLSDNG-ASAEPG-WANASNtpfrlYKQASHeggirTPLI-------VSWPKGIKA----------------KGGIRHQ 305
|
330 340
....*....|....*....|
gi 1622970030 310 LVELVSLFPTLAGLAGLQVP 329
Cdd:cd16025 306 FAHVIDIAPTILELAGVEYP 325
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
25-349 |
9.30e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 60.82 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 25 NFSTIPQYFKENGYVTMsvgkVFHPGitsnhtddSPYSWSFPPYHPSsEKYENTKtcrgpDGElhanllcpvDVVDVPEG 104
Cdd:COG1368 310 NFPSLPSILKKQGYETS----FFHGG--------DGSFWNRDSFYKN-LGFDEFY-----DRE---------DFDDPFDG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 105 T--LPDKQSTEQAIQLLEKMKtsaSPFFLAV----GyhkpHIPFRYPKEFQKLYPLENITLapdsevpdglppvaynpwm 178
Cdd:COG1368 363 GwgVSDEDLFDKALEELEKLK---KPFFAFLitlsN----HGPYTLPEEDKKIPDYGKTTL------------------- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 179 dirqredvqalnisvpygpipvefqrkirQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGwalGEHGEWAKY 258
Cdd:COG1368 417 -----------------------------NNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG---PRSPGKTDY 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 259 SNFDVATHVPLMFYVPGrtaslpeageklfpyldpfdsaseLMEPGRQSmDLVELVSLFPTLAGLAGLQVPPRcpvPSFh 338
Cdd:COG1368 465 ENPLERYRVPLLIYSPG------------------------LKKPKVID-TVGSQIDIAPTLLDLLGIDYPSY---YAF- 515
|
330
....*....|.
gi 1622970030 339 velcreGKNLL 349
Cdd:COG1368 516 ------GRDLL 520
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
25-325 |
1.38e-08 |
|
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: 55.77 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 25 NFSTIPQYFKENGYVTMSvgkvFHPGitsnhtddSPYSWSFPPYHP--------SSEKYENTKTCRGPDGelhanllcpv 96
Cdd:cd16015 79 PLPSLPSILKEQGYETIF----IHGG--------DASFYNRDSVYPnlgfdefyDLEDFPDDEKETNGWG---------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 97 dvvdvpegtLPDKQSTEQAIQLLEKMKtsASPFFLAV----GyhkpHIPFRYPKEFQKLyplenitlapdsevpdglppv 172
Cdd:cd16015 137 ---------VSDESLFDQALEELEELK--KKPFFIFLvtmsN----HGPYDLPEEKKDE--------------------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 173 aynpwmdirqredvqalnisvpygPIPVEFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWALGEH 252
Cdd:cd16015 181 ------------------------PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622970030 253 GEWAKYSNFDvATHVPLMFYVPGrtaslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAG 325
Cdd:cd16015 237 YDETDEDPLD-LYRTPLLIYSPG-------------------------LKKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
210-329 |
1.86e-08 |
|
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: 56.53 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 210 YFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL------GEHGEW-------AKYSNFDVATHVPLMFYVPGR 276
Cdd:cd16159 281 YGDNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvgGEYGGGnggiyggKKMGGWEGGIRVPTIVRWPGV 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622970030 277 tasLPeageklfpyldpfdSASELMEPGRQsMDlvelvsLFPTLAGLAGLQVP 329
Cdd:cd16159 361 ---IP--------------PGSVIDEPTSL-MD------IFPTVAALAGAPLP 389
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
27-329 |
5.34e-07 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 51.58 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 27 STIPQYFKEN----GYVTMSVGKvFHPGITSNHTDDSPYSWSFPPYHPS--SEKYENTKTCRGpdgelhanllcpvdvVD 100
Cdd:cd16154 80 ETLLQLLIKDattaGYSSAVIGK-WHLGGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNG---------------QT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 101 VPEGTLPDKQSTEQAIQLLEKmktSASPFFLAVGYHKPHIPFRYPkefqklyP--LENITLAPDSevpdglPPVAYNPwm 178
Cdd:cd16154 144 TNSTEYATTKLTNLAIDWIDQ---QTKPWFLWLAYNAPHTPFHLP-------PaeLHSRSLLGDS------ADIEANP-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 179 dirqredvqalnisvpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANsTIVAFTSDHG--------WALG 250
Cdd:cd16154 206 ----------------------------RPYYLAAIEAMDTEIGRLLASIDEEEREN-TIIIFIGDNGtpgqvvdlPYTR 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622970030 251 EHgewAKYSNFDVATHVPLMFyvpgrtaslpeageklfpyldpfdSASELMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16154 257 NH---AKGSLYEGGINVPLIV------------------------SGAGVERANERESALVNATDLYATIAELAGVDAA 308
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
207-329 |
1.00e-06 |
|
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: 50.93 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 207 RQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL-------GEHGEW--AKYSNFDVATHVPLMFYVPGRt 277
Cdd:cd16157 223 RGLYGDAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALisapeqgGSNGPFlcGKQTTFEGGMREPAIAWWPGH- 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622970030 278 aslpeageklfpyldpfdsaselMEPGRQSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16157 302 -----------------------IKPGQVSHQLGSLMDLFTTSLALAGLPIP 330
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
212-275 |
5.20e-06 |
|
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: 47.96 E-value: 5.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622970030 212 ASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWA-LGEHGewakYSNFDVATHVPLMFYVPG 275
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTdVGTHG----YDNELPDMRAIFIARGPA 243
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
28-329 |
4.14e-05 |
|
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: 45.88 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 28 TIPQYFKENGYVTMSVGKvFHPGITSNHTDDSPYswsFPPYH---------PssekYENTKTCrgPDGELHanllcpVDV 98
Cdd:cd16160 89 TMAEALKEAGYTTGMVGK-WHLGINENNHSDGAH---LPSHHgfdfvgtnlP----FTNSWAC--DDTGRH------VDF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 99 VDVPEGTLPDK-QSTEQAIQ---LLEKMKTSA---------SPFFLAVGYHKPHIPFRYPKEFQklyplenitlapdsev 165
Cdd:cd16160 153 PDRSACFLYYNdTIVEQPIQhehLTETLVGDAksfiednqeNPFFLYFSFPQTHTPLFASKRFK---------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 166 pdglppvaynpwmdirqredvqalNISVpygpipvefqrkiRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDH 245
Cdd:cd16160 217 ------------------------GKSK-------------RGRYGDNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 246 GWAL---GEHGEWA-----KYSNFDVATHVPLMFYVPGRTaslpeageklfpyldpfdsaselmePGRQSMDLVELVSLF 317
Cdd:cd16160 260 GPHVeycLEGGSTGglkggKGNSWEGGIRVPFIAYWPGTI-------------------------KPRVSHEVVSTMDIF 314
|
330
....*....|..
gi 1622970030 318 PTLAGLAGLQVP 329
Cdd:cd16160 315 PTFVDLAGGTLP 326
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
139-327 |
9.55e-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: 44.15 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 139 HIPF--RYPKEFQKLYPlenitlapdsevpdglppvaynpwmdirqredvqalnisVPYGPIPVEFQRKIRQSYFASVSY 216
Cdd:cd16017 154 HGPYydRYPEEFAKFTP---------------------------------------DCDNELQSCSKEELINAYDNSILY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 217 LDTQVGRLLSALDDLQlaNSTIVAFTSDHGWALGEHGEW--AKYSNFDVATHVPLMFYVPGRTASLPEAGEKLFPYLDPF 294
Cdd:cd16017 195 TDYVLSQIIERLKKKD--KDAALIYFSDHGESLGENGLYlhGAPYAPKEQYHVPFIIWSSDSYKQRYPVERLRANKDRPF 272
|
170 180 190
....*....|....*....|....*....|...
gi 1622970030 295 dsaselmepgrqSMDLvelvsLFPTLAGLAGLQ 327
Cdd:cd16017 273 ------------SHDN-----LFHTLLGLLGIK 288
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
204-329 |
1.25e-04 |
|
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: 44.36 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622970030 204 RKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHGWAL------GEHG--EWAKYSNFDVATHVPLMFYVPG 275
Cdd:cd16158 222 RSSRGPFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTmrksrgGNAGllKCGKGTTYEGGVREPAIAYWPG 301
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622970030 276 RTAslpeageklfpyldpfdsaselmePGRqSMDLVELVSLFPTLAGLAGLQVP 329
Cdd:cd16158 302 RIK------------------------PGV-THELASTLDILPTIAKLAGAPLP 330
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| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
210-246 |
3.92e-04 |
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c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 42.43 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1622970030 210 YFASVSYLDTQVGRLLSALDDLQLANSTIVAFTSDHG 246
Cdd:COG1524 207 YRAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
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