|
Name |
Accession |
Description |
Interval |
E-value |
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
10-508 |
0e+00 |
|
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: 574.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 10 KKPNFLVIVADDLGWSDVSPFGSEIHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGLGQMAETVrrfskv 89
Cdd:cd16025 1 GRPNILLILADDLGFSDLGCFGGEIPTPNLDALAAEGLRFTNFHTTALCSPTRAALLTGRNHHQVGMGTMAELA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 wGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLtpdrypskrgfkesfallpgggnhfayepgtrenpavpflp 169
Cdd:cd16025 75 -TGKPGYEGYLPDSAATIAEVLKDAGYHTYMSGKWHLGP----------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 plythnhdpvdhkslKNFYSSNYFAEKLIDQLK-NREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEGPDVLRKNR 248
Cdd:cd16025 113 ---------------DDYYSTDDLTDKAIEYIDeQKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGKYDAGWDALREER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 249 LQAQKDLGLIPENVIPAPVDGmGTKSWDELTTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDN 328
Cdd:cd16025 178 LERQKELGLIPADTKLTPRPP-GVPAWDSLSPEEKKLEARRMEVYAAMVEHMDQQIGRLIDYLKELGELDNTLIIFLSDN 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 329 GAEGSvleaipvlstkppvkyfdnslenlgnynsfiwygPRWAQAATAPSRLSKGFITEGGIRCPAIIRYPPLIK-PDII 407
Cdd:cd16025 257 GASAE----------------------------------PGWANASNTPFRLYKQASHEGGIRTPLIVSWPKGIKaKGGI 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 408 SDEFVTVMDILPTILELAEVPHPGHkFQGRDVVIPRGKPWIDHFvHGKPVHKDTDFSGWELFGQRAIRKGNYKAIYVPKE 487
Cdd:cd16025 303 RHQFAHVIDIAPTILELAGVEYPKT-VNGVPQLPLDGVSLLPTL-DGAAAPSRRRTQYFELFGNRAIRKGGWKAVALHPP 380
|
490 500
....*....|....*....|..
gi 19111838 488 GIKT-EWELYDLSQDKGELENL 508
Cdd:cd16025 381 PGWGdQWELYDLAKDPSETHDL 402
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
5-532 |
1.19e-114 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 345.71 E-value: 1.19e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 5 KQAESKKPNFLVIVADDLGWSDVSPFGS-EIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGTDNHIAGlgqmaet 82
Cdd:COG3119 17 AAAAAKRPNILFILADDLGYGDLGCYGNpLIKTPNIDRLAAEGVRFTNAYVTSPvCSPSRASLLTGRYPHRTG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 83 vrrfskVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLgltpdrypskrgfkesfallpgggnhfayepgtren 162
Cdd:COG3119 90 ------VTDNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKWHL------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 163 pavpflpplythnhdpvdhkslknfYSSNYFAEKLIDQLK-NREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEgp 241
Cdd:COG3119 128 -------------------------YLTDLLTDKAIDFLErQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIP-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 242 dvlrknrlqaqkdlglIPENVIPAPvdgmgtkswdelttEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTF 321
Cdd:COG3119 181 ----------------LPPNLAPRD--------------LTEEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 322 VIFMSDNGAEgsvleaipvlstkppvkyfdnslenLGNYNsFIWYgprwaqaatapsrlsKGFITEGGIRCPAIIRYPPL 401
Cdd:COG3119 231 VVFTSDNGPS-------------------------LGEHG-LRGG---------------KGTLYEGGIRVPLIVRWPGK 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 402 IKPDIISDEFVTVMDILPTILELAEVPHPGHkFQGRDVViprgkpwiDHFVHGKPVHKDTDFSGW-ELFGQRAIRKGNYK 480
Cdd:COG3119 270 IKAGSVSDALVSLIDLLPTLLDLAGVPIPED-LDGRSLL--------PLLTGEKAEWRDYLYWEYpRGGGNRAIRTGRWK 340
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 19111838 481 AIYVPKEgiKTEWELYDLSQDKGELENLAKVHPDILNELIEYWLVYEAETGV 532
Cdd:COG3119 341 LIRYYDD--DGPWELYDLKNDPGETNNLAADYPEVVAELRALLEAWLKELGD 390
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-519 |
1.15e-94 |
|
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: 295.22 E-value: 1.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEIH-TPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSG--------TDnHIAGLGqmae 81
Cdd:cd16144 1 PNIVLILVDDLGWADLGCYGSKFYeTPNIDRLAKEGMRFTQAYAAAPvCSPSRASILTGqyparlgiTD-VIPGRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 82 tvRRFSKVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFAllpGGGNHFayePGTRE 161
Cdd:cd16144 76 --GPPDNTKLIPPPSTTRLPLEEVTIAEALKDAGYATAHFGKWHLGGEGGYGPEDQGFDVNIG---GTGNGG---PPSYY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 162 NPAVPFLPPLYTHNHDPvdhkslknfYSSNYFAEKLIDQLKNReKSQSFFAYLPFTAPHWPLQSPKEYINKYRgrysegp 241
Cdd:cd16144 148 FPPGKPNPDLEDGPEGE---------YLTDRLTDEAIDFIEQN-KDKPFFLYLSHYAVHTPIQARPELIEKYE------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 242 dvlrknrlqaQKDLGLIPENVIPapvdgmgtkswdeltteekefsartmeVYAAMVELLDLNIGRVIDYLKTIGELDNTF 321
Cdd:cd16144 211 ----------KKKKGLRKGQKNP---------------------------VYAAMIESLDESVGRILDALEELGLADNTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 322 VIFMSDNGAegsvLEAIPVLSTkppvkyfDNslenlgnynsfiwygprwaqaatAPSRLSKGFITEGGIRCPAIIRYPPL 401
Cdd:cd16144 254 VIFTSDNGG----LSTRGGPPT-------SN-----------------------APLRGGKGSLYEGGIRVPLIVRWPGV 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 402 IKPDIISDEFVTVMDILPTILELAEVPHP-GHKFQGRDVViP--RGKP---------WidHFVHgkpvhkdtdFSGWELF 469
Cdd:cd16144 300 IKPGSVSDVPVIGTDLYPTFLELAGGPLPpPQHLDGVSLV-PllKGGEadlprralfW--HFPH---------YHGQGGR 367
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 19111838 470 GQRAIRKGNYKAIYVPKEGiktEWELYDLSQDKGELENLAKVHPDILNEL 519
Cdd:cd16144 368 PASAIRKGDWKLIEFYEDG---RVELYNLKNDIGETNNLAAEMPEKAAEL 414
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
12-519 |
1.99e-83 |
|
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: 265.57 E-value: 1.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGlgqmaetvrrfskVW 90
Cdd:cd16146 1 PNVILILTDDQGYGDLGFHGNPiLKTPNLDRLAAESVRFTNFHVSPVCAPTRAALLTGRYPFRTG-------------VW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 91 GGKPGYEgYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFALLPGGGNHFAYEPG-TRENPAvpflp 169
Cdd:cd16146 68 HTILGRE-RMRLDETTLAEVFKDAGYRTGIFGKWHLGDNYPYRPQDRGFDEVLGHGGGGIGQYPDYWGnDYFDDT----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 plYTHNHDPVDHKSlknfYSSNYFAEKLIDQLKnREKSQSFFAYLPFTAPHWPLQSPKEYINKYRgrysegpdvlrknrl 249
Cdd:cd16146 142 --YYHNGKFVKTEG----YCTDVFFDEAIDFIE-ENKDKPFFAYLATNAPHGPLQVPDKYLDPYK--------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 250 qaqkdlglipenvipapvdgmgtkswdeltteEKEFSARTMEVYaAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNG 329
Cdd:cd16146 200 --------------------------------DMGLDDKLAAFY-GMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 330 AEGSVLEaipvlstkppvkyfdnslenlgnynsfiwygpRWaqaaTAPSRLSKGFITEGGIRCPAIIRYPPLIKPDIISD 409
Cdd:cd16146 247 PAGGVPK--------------------------------RF----NAGMRGKKGSVYEGGHRVPFFIRWPGKILAGKDVD 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 410 EFVTVMDILPTILELAEVPHPGH-KFQGRDVV-IPRGK--PWIDH--FVHGKPVHKDTDFsgwelFGQRAIRKGNYKAIy 483
Cdd:cd16146 291 TLTAHIDLLPTLLDLCGVKLPEGiKLDGRSLLpLLKGEsdPWPERtlFTHSGRWPPPPKK-----KRNAAVRTGRWRLV- 364
|
490 500 510
....*....|....*....|....*....|....*.
gi 19111838 484 vpkEGIKTEWELYDLSQDKGELENLAKVHPDILNEL 519
Cdd:cd16146 365 ---SPKGFQPELYDIENDPGEENDVADEHPEVVKRL 397
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
11-509 |
8.27e-81 |
|
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: 258.65 E-value: 8.27e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGTDNHIAGLGQmaetvrrfsk 88
Cdd:cd16026 1 KPNIVVILADDLGYGDLGCYGSPlIKTPNIDRLAAEGVRFTDFYAAAPvCSPSRAALLTGRYPVRVGLPG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 vWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFALLpgGGNHFAYEPGTRENPAVPFL 168
Cdd:cd16026 71 -VVGPPGSKGGLPPDEITIAEVLKKAGYRTALVGKWHLGHQPEFLPTRHGFDEYFGIP--YSNDMWPFPLYRNDPPGPLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 169 PPLYTHN--HDPVDHKSLknfysSNYFAEKLIDQLKnREKSQSFFAYLPFTAPHWPLQSPKeyinKYRGRysegpdvlrk 246
Cdd:cd16026 148 PLMENEEviEQPADQSSL-----TQRYTDEAVDFIE-RNKDQPFFLYLAHTMPHVPLFASE----KFKGR---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 247 nrlqaqkdlglipenvipapvdgmgtkswdeltteekefSARTmeVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMS 326
Cdd:cd16026 208 ---------------------------------------SGAG--LYGDVVEELDWSVGRILDALKELGLEENTLVIFTS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 327 DNGAegsvleaipvlstkppvkyfdnslenlgnynsfiWYGPRWAQAATAPSRLSKGFITEGGIRCPAIIRYPPLIKPDI 406
Cdd:cd16026 247 DNGP----------------------------------WLEYGGHGGSAGPLRGGKGTTWEGGVRVPFIAWWPGVIPAGT 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 407 ISDEFVTVMDILPTILELAEVPHP-GHKFQGRDvviprgkpwIDHFVHGKPVHKDTDF----SGWELFgqrAIRKGNYKA 481
Cdd:cd16026 293 VSDELASTMDLLPTLAALAGAPLPeDRVIDGKD---------ISPLLLGGSKSPPHPFfyyyDGGDLQ---AVRSGRWKL 360
|
490 500 510
....*....|....*....|....*....|....*....
gi 19111838 482 I-----------YVPKEGIKTEWELYDLSQDKGELENLA 509
Cdd:cd16026 361 HlpttyrtgtdpGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-513 |
1.54e-78 |
|
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: 252.90 E-value: 1.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSG-TDNHiaglgqmaetvrrfSK 88
Cdd:cd16145 1 PNIIFILADDLGYGDLGCYGQKkIKTPNLDRLAAEGMRFTQHYAGAPvCAPSRASLLTGlHTGH--------------TR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 VWG-GKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLG-LTPDRYPSKRGFKESFALLPGGGNHFAYEPGTRENPAVP 166
Cdd:cd16145 67 VRGnSEPGGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGgPGTPGHPTKQGFDYFYGYLDQVHAHNYYPEYLWRNGEKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 167 FLPPLYTHNHDPVDHKSLKNF-YSSNYFAEKLIDQLKnREKSQSFFAYLPFTAPHWPLQSPKEYINKYRgrysegpdvlr 245
Cdd:cd16145 147 PLPNNVIPPLDEGNNAGGGGGtYSHDLFTDEALDFIR-ENKDKPFFLYLAYTLPHAPLQVPDDGPYKYK----------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 246 knrlqaqkdlglipenviPAPVDGMGTKSWDELtteEKEfsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFM 325
Cdd:cd16145 215 ------------------PKDPGIYAYLPWPQP---EKA--------YAAMVTRLDRDVGRILALLKELGIDENTLVVFT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 326 SDNGAEgsvleaipvlstkppvKYFDNSLenlgNYNSFIWYGPRWAqaatapsrlSKGFITEGGIRCPAIIRYPPLIKPD 405
Cdd:cd16145 266 SDNGPH----------------SEGGSEH----DPDFFDSNGPLRG---------YKRSLYEGGIRVPFIARWPGKIPAG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 406 IISDEFVTVMDILPTILELAEVPHPGHKfQGRDVViP--RGKPwidhfvhGKPVHKDTDFSGWELFGQRAIRKGNYKAIY 483
Cdd:cd16145 317 SVSDHPSAFWDFMPTLADLAGAEPPEDI-DGISLL-PtlLGKP-------QQQQHDYLYWEFYEGGGAQAVRMGGWKAVR 387
|
490 500 510
....*....|....*....|....*....|
gi 19111838 484 VPKEgiKTEWELYDLSQDKGELENLAKVHP 513
Cdd:cd16145 388 HGKK--DGPFELYDLSTDPGETNNLAAQHP 415
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
12-519 |
7.69e-73 |
|
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: 236.64 E-value: 7.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGTDNHIAGLGQMAetvrrfskvW 90
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPvCSPSRSALLTGLYPHQNGAHGLR---------S 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 91 GGKPgyegyLNDRVAALPEILQEAGYYTTMSGKWHlgltpdrypskrgfkesfallpgggnhfayepgtrENPAVPFlPP 170
Cdd:cd16027 72 RGFP-----LPDGVKTLPELLREAGYYTGLIGKTH-----------------------------------YNPDAVF-PF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 171 LYTHNHDPVDHKslknfySSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRgrysegpdvlrknrlq 250
Cdd:cd16027 111 DDEMRGPDDGGR------NAWDYASNAADFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYD---------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 251 aqkdlgliPENVIPAP--VDgmgtkswdeltTEE--KEFSArtmevYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMS 326
Cdd:cd16027 169 --------PEKVKVPPylPD-----------TPEvrEDLAD-----YYDEIERLDQQVGEILDELEEDGLLDNTIVIFTS 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 327 DNGAegsvleaipvlstkppvkyfdnslenlgnynSFiwygPRwaqaatapsrlSKGFITEGGIRCPAIIRYPPLIKPDI 406
Cdd:cd16027 225 DHGM-------------------------------PF----PR-----------AKGTLYDSGLRVPLIVRWPGKIKPGS 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 407 ISDEFVTVMDILPTILELAEVPHPGHkFQGRdvviprgkPWIDHFVHGKPVHKDTDFSGWELFG-----QRAIRKGNYKA 481
Cdd:cd16027 259 VSDALVSFIDLAPTLLDLAGIEPPEY-LQGR--------SFLPLLKGEKDPGRDYVFAERDRHDetydpIRSVRTGRYKY 329
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19111838 482 I--YVPkegikteWELYDLSQDKGELENLAKVHP--DILNEL 519
Cdd:cd16027 330 IrnYMP-------EELYDLKNDPDELNNLADDPEyaEVLEEL 364
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
10-519 |
1.15e-68 |
|
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: 227.80 E-value: 1.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 10 KKPNFLVIVADDLGWSDVSPFGSEI-HTPNIERLAKEGVRLTN-FHTASACSPTRSMLLSGTDNHIAGLGQMAETVRRFS 87
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCYGNPIvKTPNIDRLAKEGVRFDNaFVTTSICAPSRASILTGQYSHRHGVTDNNGPLFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVWggkpgyegylndrvaaLPEILQEAGYYTTMSGKWHLGLTPDRYPskRGFKEsFALLPGGGNHFAYEpgtrenpavpf 167
Cdd:cd16031 81 QPT----------------YPKLLRKAGYQTAFIGKWHLGSGGDLPP--PGFDY-WVSFPGQGSYYDPE----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 168 lpplythNHDPVDHKSLKNfYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGrysegpDVLRKN 247
Cdd:cd16031 131 -------FIENGKRVGQKG-YVTDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYED------VTIPEP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 248 RLQAQKDLGLIPENVIPAPVDGMGTKSWDELTTEEKEfsaRTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSD 327
Cdd:cd16031 197 ETFDDDDYAGRPEWAREQRNRIRGVLDGRFDTPEKYQ---RYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSD 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 328 NGaegsvleaipvlstkppvkYFdnslenLGNYNsfiWYGPRWAQaatapsrlskgfitEGGIRCPAIIRYPPLIKPDII 407
Cdd:cd16031 274 NG-------------------FF------LGEHG---LFDKRLMY--------------EESIRVPLIIRDPRLIKAGTV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 408 SDEFVTVMDILPTILELAEVPHPGHkFQGRDVV-IPRGKP------------WIDHFVHGKPVHkdtdfsgwelfgqRAI 474
Cdd:cd16031 312 VDALVLNIDFAPTILDLAGVPIPED-MQGRSLLpLLEGEKpvdwrkefyyeyYEEPNFHNVPTH-------------EGV 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19111838 475 RKGNYKAIYVPKEGikTEWELYDLSQDKGELENLAKV--HPDILNEL 519
Cdd:cd16031 378 RTERYKYIYYYGVW--DEEELYDLKKDPLELNNLANDpeYAEVLKEL 422
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
12-509 |
1.99e-68 |
|
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: 225.89 E-value: 1.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGLGQMAetvrrfskVW 90
Cdd:cd16029 1 PHIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQPICTPSRAALMTGRYPIHTGMQHGV--------IL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 91 GGKPgyeGYLNDRVAALPEILQEAGYYTTMSGKWHLGL-TPDRYPSKRGFKESFALLPGGGNHFAYEPGTRENPAVPFLp 169
Cdd:cd16029 73 AGEP---YGLPLNETLLPQYLKELGYATHLVGKWHLGFyTWEYTPTNRGFDSFYGYYGGAEDYYTHTSGGANDYGNDDL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 plytHNHDPVDHKSLKNfYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEGPDVLRKNrl 249
Cdd:cd16029 149 ----RDNEEPAWDYNGT-YSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKDEDRRT-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 250 qaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNG 329
Cdd:cd16029 222 -------------------------------------------YAAMVSALDESVGNVVDALKAKGMLDNTLIVFTSDNG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 330 AegsvleaipvlstkPPVKYFDNSlenlgNYnsfiwygprwaqaataPSRLSKGFITEGGIRCPAIIrYPPLIKPD--II 407
Cdd:cd16029 259 G--------------PTGGGDGGS-----NY----------------PLRGGKNTLWEGGVRVPAFV-WSPLLPPKrgTV 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 408 SDEFVTVMDILPTILELAEV-PHPGHKFQGRDVviprgkpWiDHFVHGKP-------VHKDTDFSGWelfGQRAIRKGNY 479
Cdd:cd16029 303 SDGLMHVTDWLPTLLSLAGGdPDDLPPLDGVDQ-------W-DALSGGAPsprteilLNIDDITRTT---GGAAIRVGDW 371
|
490 500 510
....*....|....*....|....*....|
gi 19111838 480 KAIyvpkegikTEWELYDLSQDKGELENLA 509
Cdd:cd16029 372 KLI--------VGKPLFNIENDPCERNDLA 393
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-509 |
4.93e-66 |
|
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: 219.77 E-value: 4.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE--IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGTDNHiaglgqmaetvRRFSK 88
Cdd:cd16143 1 PNIVIILADDLGYGDISCYNPDskIPTPNIDRLAAEGMRFTDAHSPSSvCTPSRYGLLTGRYPW-----------RSRLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 VWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLT---PDRYPSKRGFKESFAL---LPGGGNH--FAYEPGTr 160
Cdd:cd16143 70 GGVLGGFSPPLIEPDRVTLAKMLKQAGYRTAMVGKWHLGLDwkkKDGKKAATGTGKDVDYskpIKGGPLDhgFDYYFGI- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 161 enPAVPFLPPLYTHnhdpvdhkslknfyssnyfAEKLIDQlkNREKSQSFFAYLPFTAPHWPLQSPKEyinkYRGRYSEG 240
Cdd:cd16143 149 --PASEVLPTLTDK-------------------AVEFIDQ--HAKKDKPFFLYFALPAPHTPIVPSPE----FQGKSGAG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 241 PdvlrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNT 320
Cdd:cd16143 202 P---------------------------------------------------YGDFVYELDWVVGRILDALKELGLAENT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 321 FVIFMSDNGaegsvleaipvlstkpPVKYFDNSLENLGNYNSfiwygprwaqaaTAPSRLSKGFITEGGIRCPAIIRYPP 400
Cdd:cd16143 231 LVIFTSDNG----------------PSPYADYKELEKFGHDP------------SGPLRGMKADIYEGGHRVPFIVRWPG 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 401 LIKPDIISDEFVTVMDILPTILELAEVPHPGHkfQGRD------VVIPRGKPWIDHFVhgkpVHKDTDfsgwelfGQRAI 474
Cdd:cd16143 283 KIPAGSVSDQLVSLTDLFATLAAIVGQKLPDN--AAEDsfsflpALLGPKKQEVRESL----VHHSGN-------GSFAI 349
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19111838 475 RKGNYKAIYVPKEGIKTEW-----------ELYDLSQDKGELENLA 509
Cdd:cd16143 350 RKGDWKLIDGTGSGGFSYPrgkeklglppgQLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
12-438 |
1.76e-63 |
|
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: 207.67 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGS-EIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGtdnhiaglgqmaetvrRFSKV 89
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCYGNpDIKTPNLDRLAAEGVRFTNAYVASPvCSPSRASLLTG----------------RYPHR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 WG--GKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHlgltpdrypskrgfkesfallpgggnhfayepgtrenpavpf 167
Cdd:cd16022 65 HGvrGNVGNGGGLPPDEPTLAELLKEAGYRTALIGKWH------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 168 lpplythnhdpvdhkslknfyssnyfaEKLIDQLKNREKSQSFFAYLPFTAPHWPLqspkeyinkyrgrysegpdvlrkn 247
Cdd:cd16022 103 ---------------------------DEAIDFIERRDKDKPFFLYVSFNAPHPPF------------------------ 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 248 rlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmeVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSD 327
Cdd:cd16022 132 --------------------------------------------AYYAMVSAIDDQIGRILDALEELGLLDNTLIVFTSD 167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 328 NGaegsvleaipvlstkppvkyfdnslENLGNYNsfiwygprwaqaatapSRLSKGFITEGGIRCPAIIRYPPLIKPDII 407
Cdd:cd16022 168 HG-------------------------DMLGDHG----------------LRGKKGSLYEGGIRVPFIVRWPGKIPAGQV 206
|
410 420 430
....*....|....*....|....*....|.
gi 19111838 408 SDEFVTVMDILPTILELAEVPHPgHKFQGRD 438
Cdd:cd16022 207 SDALVSLLDLLPTLLDLAGIEPP-EGLDGRS 236
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
12-509 |
3.57e-60 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 203.53 E-value: 3.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEIH----TPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGLgqmaetvrrfS 87
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGrgapTPNIDRLAKEGLRFTSFYVEPSCTPGRAAFITGRHPIRTGL----------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVwgGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFallpGGGNHFayepgtrenpavpf 167
Cdd:cd16142 71 TV--GLPGSPGGLPPWEPTLAELLKDAGYATAQFGKWHLGDEDGRLPTDHGFDEFY----GNLYHT-------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 168 lpplythnhdpVDhkslknfyssNYFAEKLIDQLKNREKS-QSFFAYLPFTAPHWPLQSPKEYINKYRGRYsegpdvlrk 246
Cdd:cd16142 131 -----------ID----------EEIVDKAIDFIKRNAKAdKPFFLYVNFTKMHFPTLPSPEFEGKSSGKG--------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 247 nrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmeVYA-AMVElLDLNIGRVIDYLKTIGELDNTFVIFM 325
Cdd:cd16142 181 ---------------------------------------------KYAdSMVE-LDDHVGQILDALDELGIADNTIVIFT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 326 SDNGAEGSVleaipvlstkppvkyfdnslenlgnynsfiwygprWAQAATAPSRLSKGFITEGGIRCPAIIRYPPLIKPD 405
Cdd:cd16142 215 TDNGPEQDV-----------------------------------WPDGGYTPFRGEKGTTWEGGVRVPAIVRWPGKIKPG 259
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 406 IISDEFVTVMDILPTILELAEVPHPGHKFQGRDVVIPrGKPWIDHFVHGKPVHKDTDFSGWELFGQRAIRKGNYKAIYVP 485
Cdd:cd16142 260 RVSNEIVSHLDWFPTLAALAGAPDPKDKLLGKDRHID-GVDQSPFLLGKSEKSRRSEFFYFGEGELGAVRWKNWKVHFKA 338
|
490 500 510
....*....|....*....|....*....|....
gi 19111838 486 KEG---------IKTEW-ELYDLSQDKGELENLA 509
Cdd:cd16142 339 QEDtggptgepfYVLTFpLIFNLRRDPKERYDVT 372
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
10-519 |
3.96e-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: 3.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 10 KKPNFLVIVADDLGWSDVSPFG-SEIHTPNIERLAKEGVRLTNFHTASA-----CSPTRSMLLSGtdnhiaglgqmaetv 83
Cdd:cd16155 1 KKPNILFILADDQRADTIGALGnPEIQTPNLDRLARRGTSFTNAYNMGGwsgavCVPSRAMLMTG--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 84 rRFskVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHlgltpdrypskrgfkesfallpgggnhfayepgtrenp 163
Cdd:cd16155 66 -RT--LFHAPEGGKAAIPSDDKTWPETFKKAGYRTFATGKWH-------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 164 avpflpplythnhdpvdhkslknfyssNYFAEKLIDQLKNREKSQS-FFAYLPFTAPHWPLQSPKEYINKYrgryseGPD 242
Cdd:cd16155 105 ---------------------------NGFADAAIEFLEEYKDGDKpFFMYVAFTAPHDPRQAPPEYLDMY------PPE 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 243 VLRknrlqaqkdlglIPENVIPA-PVDGMGTKSWDELTT----EEKEFSARTMEVYaAMVELLDLNIGRVIDYLKTIGEL 317
Cdd:cd16155 152 TIP------------LPENFLPQhPFDNGEGTVRDEQLApfprTPEAVRQHLAEYY-AMITHLDAQIGRILDALEASGEL 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 318 DNTFVIFMSDNG-AEGSvleaipvlstkppvkyfdNSLenLGNYNSFiwygprwaqaatapsrlskgfitEGGIRCPAII 396
Cdd:cd16155 219 DNTIIVFTSDHGlAVGS------------------HGL--MGKQNLY-----------------------EHSMRVPLII 255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 397 RYPPlIKPDIISDEFVTVMDILPTILELAEVPHPGHkFQGRDVV-IPRGKpwidhfvhgKPVHKDTDFsGWELFGQRAIR 475
Cdd:cd16155 256 SGPG-IPKGKRRDALVYLQDVFPTLCELAGIEIPES-VEGKSLLpVIRGE---------KKAVRDTLY-GAYRDGQRAIR 323
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19111838 476 KGNYKAI-YVPKegIKTEwELYDLSQDKGELENLA--KVHPDILNEL 519
Cdd:cd16155 324 DDRWKLIiYVPG--VKRT-QLFDLKKDPDELNNLAdePEYQERLKKL 367
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-508 |
2.08e-57 |
|
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: 196.28 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHiaglgqmaetvrRFSKVW 90
Cdd:cd16151 1 PNIILIMADDLGYECIGCYGGEsYKTPNIDALAAEGVRFNNAYAQPLCTPSRVQLMTGKYNF------------RNYVVF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 91 ggkpgyeGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDR--YPSKRGFKESFALlpgggnHFAYEPGTRENPAVPFL 168
Cdd:cd16151 69 -------GYLDPKQKTFGHLLKDAGYATAIAGKWQLGGGRGDgdYPHEFGFDEYCLW------QLTETGEKYSRPATPTF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 169 PplythNHDPVDHKSLKNFYSSNYFAEKLIDQLKnREKSQSFFAYLPFTAPHWPLQspkeyinkyrgrysEGPDvlrknr 248
Cdd:cd16151 136 N-----IRNGKLLETTEGDYGPDLFADFLIDFIE-RNKDQPFFAYYPMVLVHDPFV--------------PTPD------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 249 lqaqkdlglipenvipapvdgmgTKSWDELTTEEKefsaRTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDN 328
Cdd:cd16151 190 -----------------------SPDWDPDDKRKK----DDPEYFPDMVAYMDKLVGKLVDKLEELGLRENTIIIFTGDN 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 329 GaegsvleaipvlsTKPPVkyfdNSLENLGNYNSfiwygprwaqaatapsrlSKGFITEGGIRCPAIIRYPPLIKPDIIS 408
Cdd:cd16151 243 G-------------THRPI----TSRTNGREVRG------------------GKGKTTDAGTHVPLIVNWPGLIPAGGVS 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 409 DEFVTVMDILPTILELAEVPHP-GHKFQGRDVViP--RGKP----WIDHFVHGKPVHKDtdfsgwelFGQRAIRKGNYKa 481
Cdd:cd16151 288 DDLVDFSDFLPTLAELAGAPLPeDYPLDGRSFA-PqlLGKTgsprREWIYWYYRNPHKK--------FGSRFVRTKRYK- 357
|
490 500
....*....|....*....|....*..
gi 19111838 482 IYVPKegiktewELYDLSQDKGELENL 508
Cdd:cd16151 358 LYADG-------RFFDLREDPLEKNPL 377
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-519 |
3.86e-55 |
|
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: 191.28 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEI-HTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGT--DNHiaglGQMAETVRRFS 87
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCYGNPIvKTPNIDRLAAEGVRFTNAYTPSPvCCPARASLLTGLypHEH----GVLNNVENAGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVWGGKPGYEGYlndrvaalPEILQEAGYYTTMSGKWHLGltPDRYPSKRGFKEsfallpgggnHFAYEPgTREnpavpf 167
Cdd:cd16033 77 YSRGLPPGVETF--------SEDLREAGYRNGYVGKWHVG--PEETPLDYGFDE----------YLPVET-TIE------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 168 lpplythnhdpvdhkslknfyssnYF-AEKLIDQLKN-REKSQSFFAYLPFTAPHWPLQSPKEYINKYR-------GRYS 238
Cdd:cd16033 130 ------------------------YFlADRAIEMLEElAADDKPFFLRVNFWGPHDPYIPPEPYLDMYDpediplpESFA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 239 EgpDVLRKNRLQAQKdlglipenvipapvdgmgTKSWDeLTTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELD 318
Cdd:cd16033 186 D--DFEDKPYIYRRE------------------RKRWG-VDTEDEEDWKEIIAHYWGYITLIDDAIGRILDALEELGLAD 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 319 NTFVIFMSDNGaegsvleaipvlstkppvkyfdnslENLGNYNSFIwygprwaqaatapsrlsKGFIT-EGGIRCPAIIR 397
Cdd:cd16033 245 DTLVIFTSDHG-------------------------DALGAHRLWD-----------------KGPFMyEETYRIPLIIK 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 398 YPPLIKPDIISDEFVTVMDILPTILELAEVPHPgHKFQGRDVV-IPRG---KPWIDHFVhgkpvhkdTDFSGWELFG-QR 472
Cdd:cd16033 283 WPGVIAAGQVVDEFVSLLDLAPTILDLAGVDVP-PKVDGRSLLpLLRGeqpEDWRDEVV--------TEYNGHEFYLpQR 353
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 19111838 473 AIRKGNYKAIYVPKEgiktEWELYDLSQDKGELENLA--KVHPDILNEL 519
Cdd:cd16033 354 MVRTDRYKYVFNGFD----IDELYDLESDPYELNNLIddPEYEEILREM 398
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
12-425 |
1.98e-53 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 183.39 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEIH-TPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGTDNHIAGLGQMaetvrrfskv 89
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRPtTPFLDRLAEEGLLFSNFYSGGtLTAPSRFALLTGLPPHNFGSYVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 wggkpgYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKesfallpgggnHFAYEPGTRENPAvpfLP 169
Cdd:pfam00884 71 ------TPVGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNLGFD-----------KFFGRNTGSDLYA---DP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 PLYTHNHDPvdhkslkNFYSSNYFAEKLIDQLKNreKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEGPDvlrknrl 249
Cdd:pfam00884 131 PDVPYNCSG-------GGVSDEALLDEALEFLDN--NDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKPSSCS------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 250 qaqkdlglipenvipapvdgmgtkswdeltteekefSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNG 329
Cdd:pfam00884 195 ------------------------------------EEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHG 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 330 AegsvleaipvlstkppvkyfdnSLENLGNYnsfiwygPRWAQAATAPsrlskgfitEGGIRCPAIIRYPPLIKPDIISD 409
Cdd:pfam00884 239 E----------------------SLGEGGGY-------LHGGKYDNAP---------EGGYRVPLLIWSPGGKAKGQKSE 280
|
410
....*....|....*.
gi 19111838 410 EFVTVMDILPTILELA 425
Cdd:pfam00884 281 ALVSHVDLFPTILDLA 296
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
11-508 |
8.08e-51 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 179.30 E-value: 8.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVAD-----DLG-WSDvspfgSEIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGtdnhiaglgQMAETv 83
Cdd:cd16034 1 KPNILFIFADqhraqALGcAGD-----DPVKTPNLDRLAKEGVVFTNAVSNYPvCSPYRASLLTG---------QYPLT- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 84 rrfSKVWG-GKPgyegyLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRgfkesFALLPGGGNH-----FAYEP 157
Cdd:cd16034 66 ---NGVFGnDVP-----LPPDAPTIADVLKDAGYRTGYIGKWHLDGPERNDGRAD-----DYTPPPERRHgfdywKGYEC 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 158 GTRenpavPFLPPLYTHNHDPVDHKSlknfYSSNYFAEKLIDQLKNR-EKSQSFFAYLPFTAPHWPLQSPKEyinKYRGR 236
Cdd:cd16034 133 NHD-----HNNPHYYDDDGKRIYIKG----YSPDAETDLAIEYLENQaDKDKPFALVLSWNPPHDPYTTAPE---EYLDM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 237 YSEGPDVLRKNrlqaqkdlglIPENvipapvdgmgtkswdeltTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGE 316
Cdd:cd16034 201 YDPKKLLLRPN----------VPED------------------KKEEAGLREDLRGYYAMITALDDNIGRLLDALKELGL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 317 LDNTFVIFMSDNGaegsvleaipvlstkppvkyfdnslENLGNYNsfiwygprwaqaatapsRLSKGFITEGGIRCPAII 396
Cdd:cd16034 253 LENTIVVFTSDHG-------------------------DMLGSHG-----------------LMNKQVPYEESIRVPFII 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 397 RYPPLIKPDIISDEFVTVMDILPTILELAEVPHPGHkFQGRDV--VIPRGKPWIDHFVHGKPVHKDTDFSGWELFGQRAI 474
Cdd:cd16034 291 RYPGKIKAGRVVDLLINTVDIMPTLLGLCGLPIPDT-VEGRDLspLLLGGKDDEPDSVLLQCFVPFGGGSARDGGEWRGV 369
|
490 500 510
....*....|....*....|....*....|....
gi 19111838 475 RKGNYKaiYVpkEGIKTEWELYDLSQDKGELENL 508
Cdd:cd16034 370 RTDRYT--YV--RDKNGPWLLFDNEKDPYQLNNL 399
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
11-508 |
1.43e-43 |
|
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: 159.17 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGSE--IHTPNIERLAKEGVRLTNFHTA-SACSPTRSMLLSGTDNHIAGLGQ--MAETVrr 85
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPnaILTPNLDKLAAEGTRFVDWYSAaSVCSPSRASLMTGRLGLRNGVGHnfLPTSV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 86 fskvwGGKPgyegyLNDrvAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFALlpgggnhfayepgtrenpav 165
Cdd:cd16161 79 -----GGLP-----LNE--TTLAEVLRQAGYATGMIGKWHLGQREAYLPNSRGFDYYFGI-------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 166 PFlpplythNHDpvdhKSLKNFYSSnyFAEKLIDQLKNreKSQSFFAYLPFTAPHWPLQ--SPKEYINKYRGRYSegpdv 243
Cdd:cd16161 127 PF-------SHD----SSLADRYAQ--FATDFIQRASA--KDRPFFLYAALAHVHVPLAnlPRFQSPTSGRGPYG----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 244 lrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevyAAMVELLDLnIGRVIDYLKTIGELDNTFVI 323
Cdd:cd16161 187 --------------------------------------------------DALQEMDDL-VGQIMDAVKHAGLKDNTLTW 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 324 FMSDNGAEGSVLEAIPVLSTkppvkyfdnslenlGNYNSFIwygprwaqaataPSRLSKGFITEGGIRCPAIIRYPPLIK 403
Cdd:cd16161 216 FTSDNGPWEVKCELAVGPGT--------------GDWQGNL------------GGSVAKASTWEGGHREPAIVYWPGRIP 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 404 PDIISDEFVTVMDILPTILELAEVPHP-GHKFQGRD---VVIPRGKPWIDHFVHGKPVHKDTDfsgwelfGQRAIRKGNY 479
Cdd:cd16161 270 ANSTSAALVSTLDIFPTVVALAGASLPpGRIYDGKDlspVLFGGSKTGHRCLFHPNSGAAGAG-------ALSAVRCGDY 342
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19111838 480 KAIYVPKEGIKTE----WELY-------DLSQDKGELENL 508
Cdd:cd16161 343 KAHYATGGALACCgstgPKLYhdppllfDLEVDPAESFPL 382
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
11-483 |
1.36e-41 |
|
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: 155.70 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGsEIH--TPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSG---------TDNHIAGLGQ 78
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFG-EPSreTPNLDRMAAEGMLFTDFYSANPlCSPSRAALLTGrlpirngfyTTNAHARNAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 79 MAEtvrrfsKVWGGKPgyegylnDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFallpGGGN-HFayep 157
Cdd:cd16157 80 TPQ------NIVGGIP-------DSEILLPELLKKAGYRNKIVGKWHLGHRPQYHPLKHGFDEWF----GAPNcHF---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 158 GTRENPAVPFLpPLYT--------HNHDPVDHKSLKNFYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEY 229
Cdd:cd16157 139 GPYDNKAYPNI-PVYRdwemigryYEEFKIDKKTGESNLTQIYLQEALEFIEKQHDAQKPFFLYWAPDATHAPVYASKPF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 230 INKY-RGRYSegpDVLRKnrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevyaamvelLDLNIGRVI 308
Cdd:cd16157 218 LGTSqRGLYG---DAVME-----------------------------------------------------LDSSVGKIL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 309 DYLKTIGELDNTFVIFMSDNGAEgsvleaipvlstkppvkyfdnslenlgnynsfiWYGPRWAQAATAPSRLSKGFITEG 388
Cdd:cd16157 242 ESLKSLGIENNTFVFFSSDNGAA---------------------------------LISAPEQGGSNGPFLCGKQTTFEG 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 389 GIRCPAIIRYPPLIKPDIISDEFVTVMDILPTILELAEVPHPghkfqgRDVVIPrGKPWIDHFVHGKPVHKDTDF-SGWE 467
Cdd:cd16157 289 GMREPAIAWWPGHIKPGQVSHQLGSLMDLFTTSLALAGLPIP------SDRAID-GIDLLPVLLNGKEKDRPIFYyRGDE 361
|
490
....*....|....*.
gi 19111838 468 LFgqrAIRKGNYKAIY 483
Cdd:cd16157 362 LM---AVRLGQYKAHF 374
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
7-509 |
6.10e-40 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 151.75 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 7 AESKKPNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGTD--NHiaglgqmaet 82
Cdd:PRK13759 2 VQTKKPNIILIMVDQMRGDCLGCNGNKaVETPNLDMLASEGYNFENAYSAVpSCTPARAALLTGLSqwHH---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 83 vrrfskvwgGKPGYegylNDRVA-----ALPEILQEAGYYTTMSGKWHLglTPDRypSKRGFKEsfALLPGGGNHFAY-E 156
Cdd:PRK13759 72 ---------GRVGY----GDVVPwnyknTLPQEFRDAGYYTQCIGKMHV--FPQR--NLLGFHN--VLLHDGYLHSGRnE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 157 PGTRENPAVPFLPPLYT----HNHDPVDH------------KSLKNFYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPH 220
Cdd:PRK13759 133 DKSQFDFVSDYLAWLREkapgKDPDLTDIgwdcnswvarpwDLEERLHPTNWVGSESIEFLRRRDPTKPFFLKMSFARPH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 221 WPLQSPKEYINKYRGRysEGPDVLRKNRLQAQKdlgLIPENVIP-APVDGMGtkswdeltteeKEFSARTMEVYAAMVEL 299
Cdd:PRK13759 213 SPYDPPKRYFDMYKDA--DIPDPHIGDWEYAED---QDPEGGSIdALRGNLG-----------EEYARRARAAYYGLITH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 300 LDLNIGRVIDYLKTIGELDNTFVIFMSDNGaegsvleaipvlstkppvkyfdnslENLGNYNSFiwygprwaqaatapsr 379
Cdd:PRK13759 277 IDHQIGRFLQALKEFGLLDNTIILFVSDHG-------------------------DMLGDHYLF---------------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 380 lSKGFITEGGIRCPAIIRYPP-LIKPD--IISDEFVTVMDILPTILELAEVPHPgHKFQGRDVV-IPRGK-----PWID- 449
Cdd:PRK13759 316 -RKGYPYEGSAHIPFIIYDPGgLLAGNrgTVIDQVVELRDIMPTLLDLAGGTIP-DDVDGRSLKnLIFGQyegwrPYLHg 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19111838 450 -HFVHGKPVHKDTDfsgwelfgqrairkGNYKAIYVPKEGiktEWELYDLSQDKGELENLA 509
Cdd:PRK13759 394 eHALGYSSDNYLTD--------------GKWKYIWFSQTG---EEQLFDLKKDPHELHNLS 437
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
11-432 |
7.77e-39 |
|
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: 147.58 E-value: 7.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGSEIHTPN-IERLAKEGVRLTN-FHTASACSPTRSMLLSGTDNHIAGL-GQMaetvrRFS 87
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASYGHPTQERGpIDDMAAEGIRFTQaYSADSVCTPSRAALLTGRLPIRSGMyGGT-----RVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVW--GGKPGYEgylndrvAALPEILQEAGYYTTMSGKWHLGLTPDRY------PSKRGFKESFALLPgGGNHFAYEPGT 159
Cdd:cd16160 76 LPWdiGGLPKTE-------VTMAEALKEAGYTTGMVGKWHLGINENNHsdgahlPSHHGFDFVGTNLP-FTNSWACDDTG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 160 R----ENPAVPFLPPLYTHNHDPVDHKSLknfyssnyfAEKLIDQLK-----NREKsqSFFAYLPFTAPHWPLQSPKEYI 230
Cdd:cd16160 148 RhvdfPDRSACFLYYNDTIVEQPIQHEHL---------TETLVGDAKsfiedNQEN--PFFLYFSFPQTHTPLFASKRFK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 231 NK-YRGRYSegpdvlrknrlqaqkdlglipenvipapvDGMGTKSWdeltteekefsartmevyaamvelldlNIGRVID 309
Cdd:cd16160 217 GKsKRGRYG-----------------------------DNINEMSW---------------------------AVGEVLD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 310 YLKTIGELDNTFVIFMSDNGaegsvleaipvlstkPPVKYFDNSlenlgnynsfiwygprwaqAATAPSRLSKGFITEGG 389
Cdd:cd16160 241 TLVDTGLDQNTLVFFLSDHG---------------PHVEYCLEG-------------------GSTGGLKGGKGNSWEGG 286
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 19111838 390 IRCPAIIRYPPLIKPDiISDEFVTVMDILPTILELA--EVPHPGH 432
Cdd:cd16160 287 IRVPFIAYWPGTIKPR-VSHEVVSTMDIFPTFVDLAggTLPTDRI 330
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
12-509 |
5.72e-38 |
|
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: 145.48 E-value: 5.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWsDVSPFG--SEIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSG--TDNHIAglgqmaetvrrf 86
Cdd:cd16028 1 RNVLFITADQWRA-DCLSCLghPLVKTPNLDRLAAEGVRFRNHYTQAApCGPSRASLYTGryLMNHRS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 87 skVWGGKPgyegyLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDrypskrgfkesfALLPGGGNHFAYE---PGTRENP 163
Cdd:cd16028 68 --VWNGTP-----LDARHLTLALELRKAGYDPALFGYTDTSPDPR------------GLAPLDPRLLSYElamPGFDPVD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 164 AVPFLPplythnhdpvdhkslKNFYSSNYFAEKLIDQLKNREKsQSFFAYLPFTAPHWPLQSPKEYINKYRGrySEGPDV 243
Cdd:cd16028 129 RLDEYP---------------AEDSDTAFLTDRAIEYLDERQD-EPWFLHLSYIRPHPPFVAPAPYHALYDP--ADVPPP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 244 LRKNRLQAQ-------KDLGLIPENVIPApvdgMGTKSWDELTTEEKefsARTMEVYAAMVELLDLNIGRVIDYLKTIGE 316
Cdd:cd16028 191 IRAESLAAEaaqhpllAAFLERIESLSFS----PGAANAADLDDEEV---AQMRATYLGLIAEVDDHLGRLFDYLKETGQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 317 LDNTFVIFMSDNGaegsvleaipvlstkppvkyfdnslENLGNYnsfiWYGprwaqaatapsrlSKGFITEGGIRCPAII 396
Cdd:cd16028 264 WDDTLIVFTSDHG-------------------------EQLGDH----WLW-------------GKDGFFDQAYRVPLIV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 397 RYP-PLIKPD--IISDEFVTVMDILPTILELAEVPHPgHKFQGRDVV--IPRGKP--WIDHfvhgkpVHKDTDFSGWELF 469
Cdd:cd16028 302 RDPrREADATrgQVVDAFTESVDVMPTILDWLGGEIP-HQCDGRSLLplLAGAQPsdWRDA------VHYEYDFRDVSTR 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19111838 470 GQR-------------AIRKGNYKaiYVPKEGIKTewELYDLSQDKGELENLA 509
Cdd:cd16028 375 RPQealglspdecslaVIRDERWK--YVHFAALPP--LLFDLKNDPGELRDLA 423
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
11-510 |
2.26e-37 |
|
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: 142.30 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLgwsDVSPFGSEIHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSG--------TDNHIAGLGqmae 81
Cdd:cd16147 1 RPNIVLILTDDQ---DVELGSMDPMPKTKKLLADQGTTFTNAFVTTPlCCPSRASILTGqyahnhgvTNNSPPGGG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 82 tvrrFSKVWggkpgyEGYLNDRvaALPEILQEAGYYTTMSGK----WHLGLTPDRYPskRGFKESFALLPGGGnhfaYEP 157
Cdd:cd16147 74 ----YPKFW------QNGLERS--TLPVWLQEAGYRTAYAGKylngYGVPGGVSYVP--PGWDEWDGLVGNST----YYN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 158 GTrenpavpflpplYTHNHDPVDHKSLKNFYSSNYFAEKLIDQLKN-REKSQSFFAYLPFTAPHWPLQSPKEYINKYrgr 236
Cdd:cd16147 136 YT------------LSNGGNGKHGVSYPGDYLTDVIANKALDFLRRaAADDKPFFLVVAPPAPHGPFTPAPRYANLF--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 237 ysegPDVLRKNRlqaqkdlgliPENVIPAPVDGmgtKSW----DELTTEEKEFS-------ARTMevyAAMVELldlnIG 305
Cdd:cd16147 201 ----PNVTAPPR----------PPPNNPDVSDK---PHWlrrlPPLNPTQIAYIdelyrkrLRTL---QSVDDL----VE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 306 RVIDYLKTIGELDNTFVIFMSDNGaegsvleaipvlstkppvkYfdnsleNLGNYnsfiwygprwaqaatapsRLSKGFI 385
Cdd:cd16147 257 RLVNTLEATGQLDNTYIIYTSDNG-------------------Y------HLGQH------------------RLPPGKR 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 386 T--EGGIRCPAIIRYPPlIKPDIISDEFVTVMDILPTILELAEVPHPGHkFQGRdvviPRGKPWIDHFvhgkpvhkdtdf 463
Cdd:cd16147 294 TpyEEDIRVPLLVRGPG-IPAGVTVDQLVSNIDLAPTILDLAGAPPPSD-MDGR----SCGDSNNNTY------------ 355
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19111838 464 sgwelfgqRAIRKGNYKAIYVPKEGIKTEWELYDLSQDKGELENLAK 510
Cdd:cd16147 356 --------KCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAG 394
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-433 |
5.38e-37 |
|
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: 137.76 E-value: 5.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLG-WSDVSPFGSEIHTPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGT-------DNHIAGlGQMAET 82
Cdd:cd16149 1 PNILFILTDDQGpWALGCYGNSEAVTPNLDRLAAEGVRFENFFCTSpVCSPARASLLTGRmpsqhgiHDWIVE-GSHGKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 83 vrrfskvwggkPGYEGYLNDRVAaLPEILQEAGYYTTMSGKWHLGltpdrypskrgfkesfallpgggnhfayepgtren 162
Cdd:cd16149 80 -----------KKPEGYLEGQTT-LPEVLQDAGYRCGLSGKWHLG----------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 163 pavpflpplythnhdpvdhkslknfyssnyfAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQspkeyinkyrgrysegpd 242
Cdd:cd16149 113 -------------------------------DDAADFLRRRAEAEKPFFLSVNYTAPHSPWG------------------ 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 243 vlrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFV 322
Cdd:cd16149 144 --------------------------------------------------YFAAVTGVDRNVGRLLDELEELGLTENTLV 173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 323 IFMSDNGAegsvleaipvlstkppvkyfdnsleNLGNYNsfIWygprwaqaatapsrlSKGFIT------EGGIRCPAII 396
Cdd:cd16149 174 IFTSDNGF-------------------------NMGHHG--IW---------------GKGNGTfplnmyDNSVKVPFII 211
|
410 420 430
....*....|....*....|....*....|....*..
gi 19111838 397 RYPPLIKPDIISDEFVTVMDILPTILELAEVPHPGHK 433
Cdd:cd16149 212 RWPGVVPAGRVVDSLVSAYDFFPTLLELAGVDPPADP 248
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
10-510 |
1.20e-36 |
|
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: 141.17 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 10 KKPNFLVIVADDLGwSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSgtdnhiaglGQMAETvrrfS 87
Cdd:cd16030 1 KKPNVLFIAVDDLR-PWLGCYGGHpAKTPNIDRLAARGVLFTNAYCQQPvCGPSRASLLT---------GRRPDT----T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVWGGKPGYEGYLNDRVaALPEILQEAGYYTTMSGK-WHlGLTPDRYPSKRGFKESFallpgggNHFAYEPGTRENPAVP 166
Cdd:cd16030 67 GVYDNNSYFRKVAPDAV-TLPQYFKENGYTTAGVGKiFH-PGIPDGDDDPASWDEPP-------NPPGPEKYPPGKLCPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 167 FLPPLYTHNHDPVDHKSLK-NFYSSNYFAEKLIDQLKNR-EKSQSFFAYLPFTAPHWPLQSPKeyinKYRGRYSEGPDVL 244
Cdd:cd16030 138 KKGGKGGGGGPAWEAADVPdEAYPDGKVADEAIEQLRKLkDSDKPFFLAVGFYKPHLPFVAPK----KYFDLYPLESIPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 245 RKNrlQAQKDLGLIPENV---IPAPVDGMGTKSWDELTTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTF 321
Cdd:cd16030 214 PNP--FDPIDLPEVAWNDlddLPKYGDIPALNPGDPKGPLPDEQARELRQAYYASVSYVDAQVGRVLDALEELGLADNTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 322 VIFMSDNGaegsvleaipvlstkppvkYfdnsleNLGNYNsfiwygpRWAQAATapsrlskgFitEGGIRCPAIIRYPPL 401
Cdd:cd16030 292 VVLWSDHG-------------------W------HLGEHG-------HWGKHTL--------F--EEATRVPLIIRAPGV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 402 IKPDIISDEFVTVMDILPTILELAEVPHPGHkFQGRDVViprgkPWIDHFVHGKPVHKDTDFSGWELFGqRAIRKGNYKA 481
Cdd:cd16030 330 TKPGKVTDALVELVDIYPTLAELAGLPAPPC-LEGKSLV-----PLLKNPSAKWKDAAFSQYPRPSIMG-YSIRTERYRY 402
|
490 500 510
....*....|....*....|....*....|
gi 19111838 482 I-YVPKEGIKTEwELYDLSQDKGELENLAK 510
Cdd:cd16030 403 TeWVDFDKVGAE-ELYDHKNDPNEWKNLAN 431
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
11-486 |
2.22e-36 |
|
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: 142.04 E-value: 2.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFG-SEIHTPNIERLAKEGVRLTNfHTASA--CSPTRSMLL-------SGTDNHIAGLgqma 80
Cdd:cd16159 1 KPNIVLFMADDLGIGDVGCFGnDTIRTPNIDRLAKEGVKLTH-HLAAAplCTPSRAAFLtgrypirSGMASSHGMR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 81 etVRRFSKVWGGKPGYEgylndrvAALPEILQEAGYYTTMSGKWHLGL----TPDRY--PSKRGFkesfallpgggNHFA 154
Cdd:cd16159 76 --VILFTASSGGLPPNE-------TTFAEVLKQQGYSTALIGKWHLGLhcesRNDFChhPLNHGF-----------DYFY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 155 YEPGTRENPAVPFLPPLYTHNHDPVDHKSLKNFYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPkeYINKY- 233
Cdd:cd16159 136 GLPLTNLKDCGDGSNGEYDLSFDPLFPLLTAFVLITALTIFLLLYLGAVSKRFFVFLLILSLLFISLFFLLL--ITNRYf 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 234 ------RGRYSEGPDVLRK--NRLqAQKDLGLIPEN-------VIpapvdgmgtkSWDELTTE---EKEFSARTME-VYA 294
Cdd:cd16159 214 ncilmrNHEVVEQPMSLENltQRL-TKEAISFLERNkerpfllVM----------SFLHVHTAlftSKKFKGRSKHgRYG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 295 AMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNGAEgsvLEAIPVLStkppvkyfdnsleNLGNYNSfIWYGPRWAQaa 374
Cdd:cd16159 283 DNVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGGH---LEEISVGG-------------EYGGGNG-GIYGGKKMG-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 375 tapsrlskGFitEGGIRCPAIIRYPPLIKPDIISDEFVTVMDILPTILELAEVPHPghkfqgRDVVIPrGKPwIDHFVHG 454
Cdd:cd16159 344 --------GW--EGGIRVPTIVRWPGVIPPGSVIDEPTSLMDIFPTVAALAGAPLP------SDRIID-GRD-LMPLLTG 405
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19111838 455 KPVHKDTDF----SGWELFGQRAI-RKGN--YKAIYV-PK 486
Cdd:cd16159 406 QEKRSPHEFlfhyCGAELHAVRYRpRDGGavWKAHYFtPN 445
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
11-536 |
8.07e-36 |
|
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: 139.89 E-value: 8.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGseiH----TPNIERLAKEGVRLTNFH-TASACSPTRSMLLSGtdnhiaglgqmaetvrR 85
Cdd:cd16158 1 PPNIVLLFADDLGYGDLGCYG---HpsssTPNLDRLAANGLRFTDFYsSSPVCSPSRAALLTG----------------R 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 86 F---SKVWGG--KPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDR--YPSKRGFkESFALLPgggnhFAYEPG 158
Cdd:cd16158 62 YqvrSGVYPGvfYPGSRGGLPLNETTIAEVLKTVGYQTAMVGKWHLGVGLNGtyLPTHQGF-DHYLGIP-----YSHDQG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 159 TREN-----PAVP-------FLPPLYTHNHD-----PVDHKSLKNFYssNYFAEKLIDqlKNREKSQSFFAYLPFTAPHW 221
Cdd:cd16158 136 PCQNltcfpPNIPcfggcdqGEVPCPLFYNEsivqqPVDLLTLEERY--AKFAKDFIA--DNAKEGKPFFLYYASHHTHY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 222 PLQSPKeyinKYRGRYSEGPdvlrknrlqaqkdlglipenvipapvdgmgtkswdeltteekeFSARTMEvyaamvelLD 301
Cdd:cd16158 212 PQFAGQ----KFAGRSSRGP-------------------------------------------FGDALAE--------LD 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 302 LNIGRVIDYLKTIGELDNTFVIFMSDNGAEGSvleaipvlstkppvkyfdnslenlgnynsfiwygpRWAQAATAP-SRL 380
Cdd:cd16158 237 GSVGELLQTLKENGIDNNTLVFFTSDNGPSTM-----------------------------------RKSRGGNAGlLKC 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 381 SKGFITEGGIRCPAIIRYPPLIKPDiISDEFVTVMDILPTILELAEVPHPGHKFQGRDVViprgkpwiDHFVHGKPVHKD 460
Cdd:cd16158 282 GKGTTYEGGVREPAIAYWPGRIKPG-VTHELASTLDILPTIAKLAGAPLPNVTLDGVDMS--------PILFEQGKSPRQ 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 461 TDF----SGWELFGQRAIRKGNYKAIYVPKEGIKTEWE------------------LYDLSQDKGELENLAKVhPDILNE 518
Cdd:cd16158 353 TFFyyptSPDPDKGVFAVRWGKYKAHFYTQGAAHSGTTpdkdchpsaeltshdpplLFDLSQDPSENYNLLGL-PEYNQV 431
|
570
....*....|....*....
gi 19111838 519 LIEYWLVYEA-ETGVVTAP 536
Cdd:cd16158 432 LKQIQQVKERfEASMKFGE 450
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-501 |
1.09e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 121.88 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGtdnhiaglgqmaetvRRFSK- 88
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCYGHPvVRTPNLDRLAARGTRFENAYTPSPiCVPSRASFLTG---------------RYVHEt 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 -VWGGKPGYEGylndRVAALPEILQEAGYYTTMSGKWHLgltpdRYPSKRGFkesfallpgggnhFAY-EPGTREnpAVP 166
Cdd:cd16037 66 gVWDNADPYDG----DVPSWGHALRAAGYETVLIGKLHF-----RGEDQRHG-------------FRYdRDVTEA--AVD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 167 FLpplytHNHDPVDhkslknfyssnyfaeklidqlknreksQSFFAYLPFTAPHWPLQSPKEYINKYRgrysegpdvlrk 246
Cdd:cd16037 122 WL-----REEAADD---------------------------KPWFLFVGFVAPHFPLIAPQEFYDLYV------------ 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 247 nrlqaqkdlglipenvipapvdgmgtkswdeltteekefsARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMS 326
Cdd:cd16037 158 ----------------------------------------RRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTS 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 327 DNGaegsvleaipvlstkppvkyfdnslENLGnYNSFIWygprwaqaatapsrlsKGFITEGGIRCPAIIRYpPLIKPDI 406
Cdd:cd16037 198 DHG-------------------------DMLG-ERGLWG----------------KSTMYEESVRVPMIISG-PGIPAGK 234
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 407 ISDEFVTVMDILPTILELAEVPHPGHkfqgrdvviPRGKPWIDhFVHGKPVHKDTDFSGWELFGQ----RAIRKGNYKAI 482
Cdd:cd16037 235 RVKTPVSLVDLAPTILEAAGAPPPPD---------LDGRSLLP-LAEGPDDPDRVVFSEYHAHGSpsgaFMLRKGRWKYI 304
|
490
....*....|....*....
gi 19111838 483 YVPKEGIktewELYDLSQD 501
Cdd:cd16037 305 YYVGYPP----QLFDLEND 319
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-510 |
3.00e-28 |
|
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: 116.95 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTA-SACSPTRSMLLSGTDNHIAG---LGQMaetvrrf 86
Cdd:cd16150 1 PNIVIFVADQLRADSLGHLGNPaAVTPNLDALAAEGVRFSNAYCQnPVCSPSRCSFLTGWYPHVNGhrtLHHL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 87 skvwggkpgyegyLNDRVAALPEILQEAGYYTTMSGKWHLglTPDRYpskrgFKESFALlpgggnhfayepgtrenpavp 166
Cdd:cd16150 74 -------------LRPDEPNLLKTLKDAGYHVAWAGKNDD--LPGEF-----AAEAYCD--------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 167 flpplythnhdpVDHKslknfyssnyFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGrysEGPDVLRK 246
Cdd:cd16150 113 ------------SDEA----------CVRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDR---EKLPPRRP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 247 NRLQAQKDLGLIPenvipapvdGMGTKSWDELTTEE-KEFSArtmeVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFM 325
Cdd:cd16150 168 PGLRAKGKPSMLE---------GIEKQGLDRWSEERwRELRA----TYLGMVSRLDHQFGRLLEALKETGLYDDTAVFFF 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 326 SDNGaegsvleaipvlstkppvkyfdnslENLGNYNsfiwygprwaQAATAPSrlskGF---ITeggiRCPAIIRYPPLI 402
Cdd:cd16150 235 SDHG-------------------------DYTGDYG----------LVEKWPN----TFedcLT----RVPLIIKPPGGP 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 403 KPDiISDEFVTVMDILPTILELAEVP----HPGHKF---------QGRDVVIPRGKpwidhFVHGKPVHKDTDFSGWELF 469
Cdd:cd16150 272 AGG-VSDALVELVDIPPTLLDLAGIPlshtHFGRSLlpvlageteEHRDAVFSEGG-----RLHGEEQAMEGGHGPYDLK 345
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 19111838 470 GQR--------------AIRKGNYKAIYVPKEgiktEWELYDLSQDKGELENLAK 510
Cdd:cd16150 346 WPRllqqeeppehtkavMIRTRRYKYVYRLYE----PDELYDLEADPLELHNLIG 396
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-425 |
3.60e-28 |
|
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: 115.91 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGwSDVSP---FGSEI-HTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTdnhiaglgqmaetvrrfs 87
Cdd:cd16154 1 PNILLIIADDQG-LDSSAqysLSSDLpVTPTLDSLANSGIVFDNLWATPACSPTRATILTGK------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 kvWGGKPGYEGyLNDRVAALPEILQE--------AGYYTTMSGKWHLGLTPDRYPSKRGFKESFALLPGGGNHFaYEPGT 159
Cdd:cd16154 62 --YGFRTGVLA-VPDELLLSEETLLQllikdattAGYSSAVIGKWHLGGNDNSPNNPGGIPYYAGILGGGVQDY-YNWNL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 160 RENPAVpflpplyTHNHDpvdhkslknfYSSNYFAEKLIDQLKNreKSQSFFAYLPFTAPHWPLQSPkeyinkyrgryse 239
Cdd:cd16154 138 TNNGQT-------TNSTE----------YATTKLTNLAIDWIDQ--QTKPWFLWLAYNAPHTPFHLP------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 240 gpdvlrKNRLQAQKDLGlipenvipapvdgmgtkswdelTTEEKEFSARTmeVYAAMVELLDLNIGRVIDYLkTIGELDN 319
Cdd:cd16154 186 ------PAELHSRSLLG----------------------DSADIEANPRP--YYLAAIEAMDTEIGRLLASI-DEEEREN 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 320 TFVIFMSDNGAEGSVLEAipvlstkppvkyfdnslenlgnynsfiWYgprwaqaataPSRLSKGFITEGGIRCPAIIRYP 399
Cdd:cd16154 235 TIIIFIGDNGTPGQVVDL---------------------------PY----------TRNHAKGSLYEGGINVPLIVSGA 277
|
410 420
....*....|....*....|....*.
gi 19111838 400 PLIKPDIISDEFVTVMDILPTILELA 425
Cdd:cd16154 278 GVERANERESALVNATDLYATIAELA 303
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
11-521 |
1.58e-27 |
|
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: 114.25 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGSEIH-TPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGtdnhiaglgQMAETvrrfSK 88
Cdd:cd16152 1 KPNVIVFFTDQQRWDTLGCYGQPLDlTPNLDALAEEGVLFENAFTPQpVCGPARACLQTG---------LYPTE----TG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 VW-GGKPgyegyLNDRVAALPEILQEAGYYTTMSGKWHLGltpdrypskrgfkesfallpgggnhfayepGTRenpavpf 167
Cdd:cd16152 68 CFrNGIP-----LPADEKTLAHYFRDAGYETGYVGKWHLA------------------------------GYR------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 168 lpplythnhdpVDhkslknfyssnYFAEKLIDQLKNREKSQSFFAYLPFTAPH-----WPLQSPKEYINKYRGRYsegpd 242
Cdd:cd16152 106 -----------VD-----------ALTDFAIDYLDNRQKDKPFFLFLSYLEPHhqndrDRYVAPEGSAERFANFW----- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 243 vlrknrlqaqkdlglIPENVIPAPVDgmgtkSWDELTTeekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFV 322
Cdd:cd16152 159 ---------------VPPDLAALPGD-----WAEELPD------------YLGCCERLDENVGRIRDALKELGLYDNTII 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 323 IFMSDNGAEgsvleaipvLSTKPpvkyfdnslenlGNYnsfiwygprwaqaatapsrlsKGFITEGGIRCPAIIRYPPLI 402
Cdd:cd16152 207 VFTSDHGCH---------FRTRN------------AEY---------------------KRSCHESSIRVPLVIYGPGFN 244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 403 KPDIIsDEFVTVMDILPTILELAEVPhPGHKFQGR---DVVIPRGKPWIDhfvhgkpvhkdtdfsgwELFGQ-------R 472
Cdd:cd16152 245 GGGRV-EELVSLIDLPPTLLDAAGID-VPEEMQGRsllPLVDGKVEDWRN-----------------EVFIQisesqvgR 305
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 473 AIRKGNYK-AIYVP-KEGIK-------TEWELYDLSQDKGELENLA--KVHPDILNELIE 521
Cdd:cd16152 306 AIRTDRWKySVAAPdKDGWKdsgsdvyVEDYLYDLEADPYELVNLIgrPEYREVAAELRE 365
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
12-522 |
3.48e-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: 111.71 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFG-SEIHTPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGTDNHIAGLgqmaetvrrfskv 89
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCYGnKAMKTPNLDRLAAEGVRFDSAYTTQpVCGPARSGLFTGLYPHTNGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 WGGKPGyegyLNDRVAALPEILQEAGYYTTMSGKWHLgltpdrypskrgfkesfallpGGGNHFAY---EPGTREN---P 163
Cdd:cd16156 68 WTNCMA----LGDNVKTIGQRLSDNGIHTAYIGKWHL---------------------DGGDYFGNgicPQGWDPDywyD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 164 AVPFLPPLyTHNHDPVDHKSLKNFYSSNYFAE---------KLIDQLKNReKSQSFFAYLPFTAPHWPLQSPKEYINKYR 234
Cdd:cd16156 123 MRNYLDEL-TEEERRKSRRGLTSLEAEGIKEEftyghrctnRALDFIEKH-KDEDFFLVVSYDEPHHPFLCPKPYASMYK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 235 GRYSEgpdvLRKNrlqAQKDLGLIPENvipapvdgmgTKSW--DELTTEEKEFSARtMEVYAAMVELLDLNIGRVIDYLK 312
Cdd:cd16156 201 DFEFP----KGEN---AYDDLENKPLH----------QRLWagAKPHEDGDKGTIK-HPLYFGCNSFVDYEIGRVLDAAD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 313 TIGEldNTFVIFMSDNG-AEGSvleaiPVLSTKPPVKYFDnslenlgnynsfiwygprwaqaatapsrlskgfITeggiR 391
Cdd:cd16156 263 EIAE--DAWVIYTSDHGdMLGA-----HKLWAKGPAVYDE---------------------------------IT----N 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 392 CPAIIRYPPLIKPDIISDEFVTVMDILPTILELAEVPHPgHKFQG----RDVVIPRGKPWIDHFVHGKPVHKDTD-FSGW 466
Cdd:cd16156 299 IPLIIRGKGGEKAGTVTDTPVSHIDLAPTILDYAGIPQP-KVLEGesilATIEDPEIPENRGVFVEFGRYEVDHDgFGGF 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111838 467 ELFgqRAIRKGNYKAIYvpkeGIKTEWELYDLSQDKGELENL------AKVHPDILNELIEY 522
Cdd:cd16156 378 QPV--RCVVDGRYKLVI----NLLSTDELYDLEKDPYEMHNLiddpdyADVRDQLHDELLDY 433
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
12-501 |
3.82e-25 |
|
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.
Pssm-ID: 293756 [Multi-domain] Cd Length: 327 Bit Score: 106.12 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEI-HTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGtdnhiaglgQMAETVRRFskv 89
Cdd:cd16032 1 PNILLIMADQLTAAALPAYGNTVvKTPNLDRLAARGVVFDNAYCNSPlCAPSRASMMTG---------RLPSRIGAY--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 wggkpgyegylnDRVAALP-EI------LQEAGYYTTMSGKWHLgLTPDRYpskrgfkesfallpgggnH-FAYEpgtre 161
Cdd:cd16032 69 ------------DNAAEFPaDIptfahyLRAAGYRTALSGKMHF-VGPDQL------------------HgFDYD----- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 162 npavpflpplythnhDPVDHKSLKNFYssnyfaeklidQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYrgrysegp 241
Cdd:cd16032 113 ---------------EEVAFKAVQKLY-----------DLARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLY-------- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 242 dVLRknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsARtmEVYAAMVELLDLNIGRVIDYLKTIGELDNTF 321
Cdd:cd16032 159 -VRR-----------------------------------------AR--RAYYGMVSYVDDKVGQLLDTLERTGLADDTI 194
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 322 VIFMSDNGaegsvleaipvlstkppvkyfdnslENLGNYNsfIWYgprwaqaatapsrlsKGFITEGGIRCPAIIRYPPL 401
Cdd:cd16032 195 VIFTSDHG-------------------------DMLGERG--LWY---------------KMSFFEGSARVPLIISAPGR 232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 402 IKPDIISdEFVTVMDILPTILELAEVPHPGH--KFQGRDVViprgkpwiDHFVHGKPVHKDTDFSgwELFGQ------RA 473
Cdd:cd16032 233 FAPRRVA-EPVSLVDLLPTLVDLAGGGTAPHvpPLDGRSLL--------PLLEGGDSGGEDEVIS--EYLAEgavapcVM 301
|
490 500
....*....|....*....|....*...
gi 19111838 474 IRKGNYKAIYVPKEGIktewELYDLSQD 501
Cdd:cd16032 302 IRRGRWKFIYCPGDPD----QLFDLEAD 325
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-440 |
5.65e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 98.77 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSE-IHTPNIERLAKEGVRLTNFHTASA-CSPTRSMLLSGTDNHiaglgqmaetvrrfskV 89
Cdd:cd16148 1 MNVILIVIDSLRADHLGCYGYDrVTTPNLDRLAAEGVVFDNHYSGSNpTLPSRFSLFTGLYPF----------------Y 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 WGgkpGYEGYLNDRVAALPEILQEAGYYTtmsgkwHLGLTPDRYPSKRGFKESFallpgggnhFAYEPGtrenpavpflP 169
Cdd:cd16148 65 HG---VWGGPLEPDDPTLAEILRKAGYYT------AAVSSNPHLFGGPGFDRGF---------DTFEDF----------R 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 PLYTHNHDPVDHKSLKNFyssnyfaEKLIDQLKNREKSQSFFAYLPFTAPHWPlqspkeyinkYRgrysegpdvlrknrl 249
Cdd:cd16148 117 GQEGDPGEEGDERAERVT-------DRALEWLDRNADDDPFFLFLHYFDPHEP----------YL--------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 250 qaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNG 329
Cdd:cd16148 165 -------------------------------------------YDAEVRYVDEQIGRLLDKLKELGLLEDTLVIVTSDHG 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 330 aegsvleaipvlstkppvkyfdnslENLGNYNsfIWYGPRWAQaatapsrlskgfiTEGGIRCPAIIRYPPLiKPDIISD 409
Cdd:cd16148 202 -------------------------EEFGEHG--LYWGHGSNL-------------YDEQLHVPLIIRWPGK-EPGKRVD 240
|
410 420 430
....*....|....*....|....*....|.
gi 19111838 410 EFVTVMDILPTILELAEVPHPgHKFQGRDVV 440
Cdd:cd16148 241 ALVSHIDIAPTLLDLLGVEPP-DYSDGRSLL 270
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
12-440 |
1.19e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 89.96 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVAD-DLGWSDVSPFGSEIHTPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGTdnHIAgLGQMAETVrrfskv 89
Cdd:cd16035 1 PNILLILTDqERYPPPWPAGWAALNLPARERLAANGLSFENHYTAAcMCSPSRSTLYTGL--HPQ-QTGVTDTL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 90 wggKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGltpdrypskrgfkesfaLLPGGGnhfayepgtrenpavpflp 169
Cdd:cd16035 72 ---GSPMQPLLSPDVPTLGHMLRAAGYYTAYKGKWHLS-----------------GAAGGG------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 170 plytHNHDPVdhkslknfyssnyFAEKLIDQLKNREKS----QSFFAYLPFTAPH---WPLQSPKEYInkYRGRYsegpd 242
Cdd:cd16035 113 ----YKRDPG-------------IAAQAVEWLRERGAKnadgKPWFLVVSLVNPHdimFPPDDEERWR--RFRNF----- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 243 vlrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGELDNTFV 322
Cdd:cd16035 169 --------------------------------------------------YYNLIRDVDRQIGRVLDALDASGLADNTIV 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 323 IFMSDNGaegsvleaipvlstkppvkyfdnslENLGnynsfiwygprwaqaatAPSRLSKGF-ITEGGIRCPAIIRYPPL 401
Cdd:cd16035 199 VFTSDHG-------------------------EMGG-----------------AHGLRGKGFnAYEEALHVPLIISHPDL 236
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 19111838 402 IKPDIISDEFVTVMDILPTILELAEVPHP-----GHKFQGRDVV 440
Cdd:cd16035 237 FGTGQTTDALTSHIDLLPTLLGLAGVDAEarateAPPLPGRDLS 280
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
11-440 |
5.87e-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: 293772 [Multi-domain] Cd Length: 282 Bit Score: 87.05 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 11 KPNFLVIVADDLGWSDVSPFGS-----------EIHTPNIERLAKEGVRLTNFHTAS-ACSPTRSMLLSGTDNHIAGLGQ 78
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNNahtgksesrlgYVESPNIDALAAEGVLFTNAYCNSpVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 79 --MAETVRRFSKVwggkpgyegylndrvaALPEILQEAGYYTTMSGKWHlgltpdrypskrgfkesfallpgggnhfaYE 156
Cdd:cd16153 81 feAAHPALDHGLP----------------TFPEVLKKAGYQTASFGKSH-----------------------------LE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 157 PGTRenpavpflpplYTHNhdpvDHKSLKNFYSSNyfaEKLIDQlknrekSQSFFAYLPFTAPHWPLQSPKEYINKYRgr 236
Cdd:cd16153 116 AFQR-----------YLKN----ANQSYKSFWGKI---AKGADS------DKPFFVRLSFLQPHTPVLPPKEFRDRFD-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 237 ysegpdvlrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmevYAAMVELLDLNIGRVIDYLKTIGE 316
Cdd:cd16153 170 --------------------------------------------------------YYAFCAYGDAQVGRAVEAFKAYSL 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 317 L---DNTFVIFMSDNGAegsvleaipvlstkppvkyfdnsleNLGNYNSFIWYGPrWAQAatapsrlskgfiteggIRCP 393
Cdd:cd16153 194 KqdrDYTIVYVTGDHGW-------------------------HLGEQGILAKFTF-WPQS----------------HRVP 231
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 19111838 394 AIIRYPPLIK--PDIISDEFVTVMDILPTILELAEVPHPGHK-FQGRDVV 440
Cdd:cd16153 232 LIVVSSDKLKapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDGRDLF 281
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
12-425 |
1.19e-18 |
|
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: 85.16 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSPFGSEI-HTPNIERLAKEGVRLTNFHTASACS--PTRSMLLSGTDNHIAGLGQMAETVRrfsk 88
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPApTTPNLKRLASEGATFNFRSVSPPTSsaPNHAALLTGAYPTLHGYTGNGSADP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 89 vwgGKPGYEGYLNDRVAALPEILQEAGYYTTMsgkwhlgltpdrypskrgfkesFALLpgggnhfayepgtrenpavpfl 168
Cdd:cd00016 77 ---ELPSRAAGKDEDGPTIPELLKQAGYRTGV----------------------IGLL---------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 169 pplythnhdpvdhkslknfyssnyfaekliDQLKNREKSQSFFAYLPFTAPHWPLQSpkeyinkyrgrysegpdvlrknr 248
Cdd:cd00016 110 ------------------------------KAIDETSKEKPFVLFLHFDGPDGPGHA----------------------- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 249 lqaqkdlglipenvipapvdgmgtkswdeltteekefSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDN 328
Cdd:cd00016 137 -------------------------------------YGPNTPEYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADH 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 329 GAEGSVLEAIPVLSTKPpvkyfdnslenlgnynsfiwygprwaqaatapsrlskgFITEGGIRCPAIIRYPPLIKPDIIs 408
Cdd:cd00016 180 GGIDKGHGGDPKADGKA--------------------------------------DKSHTGMRVPFIAYGPGVKKGGVK- 220
|
410
....*....|....*..
gi 19111838 409 DEFVTVMDILPTILELA 425
Cdd:cd00016 221 HELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
4-448 |
1.21e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 63.90 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 4 NKQAESKKPNFLVIVADDLGWSDVSPFGSEIH-TPNIERLAKEGVRLTNFHTASacspTRS-----MLLSGtdnhiaglg 77
Cdd:COG1368 227 NPFGPAKKPNVVVILLESFSDFFIGALGNGKDvTPFLDSLAKESLYFGNFYSQG----GRTsrgefAVLTG--------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 78 qmaetvrrFSKVWGGKPgYEGYLNDRVAALPEILQEAGYYTTMsgkWHlgltpdrypskrGFKESF----ALLPGGG-NH 152
Cdd:COG1368 294 --------LPPLPGGSP-YKRPGQNNFPSLPSILKKQGYETSF---FH------------GGDGSFwnrdSFYKNLGfDE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 153 FayepgtrenpavpflpplythnhdpVDHKSLKNFYSSNY------FAEKLIDQLKnrEKSQSFFAYLPFTAPHWPLQSP 226
Cdd:COG1368 350 F-------------------------YDREDFDDPFDGGWgvsdedLFDKALEELE--KLKKPFFAFLITLSNHGPYTLP 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 227 KEYInkyrgRYSEGPDVLRKNRLQAQKdlglipenvipapvdgmgtkswdeltteekefsartmevYAamvellDLNIGR 306
Cdd:COG1368 403 EEDK-----KIPDYGKTTLNNYLNAVR---------------------------------------YA------DQALGE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 307 VIDYLKTIGELDNTFVIFMSDNGaegsvleaipvlstkPPVKYFDNSLENLGNYNSfiwygprwaqaatapsrlskgfit 386
Cdd:COG1368 433 FIEKLKKSGWYDNTIFVIYGDHG---------------PRSPGKTDYENPLERYRV------------------------ 473
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111838 387 eggircPAIIRYPPLIKPDIIsDEFVTVMDILPTILELAEVPHPGHKFQGRDVVIPRGKPWI 448
Cdd:COG1368 474 ------PLLIYSPGLKKPKVI-DTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLLSPDTDPFA 528
|
|
| DUF4994 |
pfam16385 |
Domain of unknown function; This family around 100 residues locates in the C-terminal of some ... |
473-519 |
8.04e-07 |
|
Domain of unknown function; This family around 100 residues locates in the C-terminal of some uncharacterized proteins in various Bacteroides and Prevotella species. The function of this family remains unknown.
Pssm-ID: 406720 [Multi-domain] Cd Length: 98 Bit Score: 47.28 E-value: 8.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 19111838 473 AIRKGNYKAI-------YVPKEGIKT----EWELYDLSQDKGELENLAKVHPDILNEL 519
Cdd:pfam16385 37 SVRTGDWKYIepsdgpaYIKWTKIETgnspEPQLYDLKADPGEQENVAKKHPEKVKEL 94
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
12-425 |
1.68e-06 |
|
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: 49.99 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 12 PNFLVIVADDLGWSDVSP-FGSEIHTPNIERLAKEGVRLTNFHTASACSPT-RSM--LLSGtdnhiaglgqmaetvrrFS 87
Cdd:cd16015 1 PNVIVILLESFSDPYIDKdVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTaNGEfeVLTG-----------------LP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 88 KVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSgkwhlgltpdrYPSKRGF---KESFALLpgGGNHFAyepgTRENpa 164
Cdd:cd16015 64 PLPLGSGSYTLYKLNPLPSLPSILKEQGYETIFI-----------HGGDASFynrDSVYPNL--GFDEFY----DLED-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 165 vpFLPPLYTHNHdpvdhkslkNFYSSNYFAEKLIDQLKNREKsQSFFAYLpFTA-PHWPLQSPKEYINKYRGRYSEGPDV 243
Cdd:cd16015 125 --FPDDEKETNG---------WGVSDESLFDQALEELEELKK-KPFFIFL-VTMsNHGPYDLPEEKKDEPLKVEEDKTEL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 244 lrknrlqaqkdlglipenvipapvdgmgtkswdeltteekefsartmEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVI 323
Cdd:cd16015 192 -----------------------------------------------ENYLNAIHYTDKALGEFIEKLKKSGLYENTIIV 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111838 324 FMSDNGAegsvleaipvlstKPPVKYFDNSLENLGNYNSfiwygprwaqaatapsrlskgfiteggircPAIIRYPPLIK 403
Cdd:cd16015 225 IYGDHLP-------------SLGSDYDETDEDPLDLYRT------------------------------PLLIYSPGLKK 261
|
410 420
....*....|....*....|..
gi 19111838 404 PDIIsDEFVTVMDILPTILELA 425
Cdd:cd16015 262 PKKI-DRVGSQIDIAPTLLDLL 282
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
472-519 |
4.60e-03 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 36.84 E-value: 4.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19111838 472 RAIRKGNYKAIYVPKEgiKTEWELYDLSQDKGELENL--AKVHPDILNEL 519
Cdd:pfam16347 43 YGVRTERYKLIHFYND--IDEWELYDLQKDPKEMNNVygDPEYAEVQAEL 90
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
1-54 |
7.72e-03 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 38.96 E-value: 7.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19111838 1 MAFNKQAESKKPNFLVIVADDLGWSDVSPFgseiHTPNIERLAKEGVRLTNFHT 54
Cdd:COG1524 13 LAAAAAAAPPAKKVVLILVDGLRADLLERA----HAPNLAALAARGVYARPLTS 62
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
293-330 |
8.76e-03 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 38.27 E-value: 8.76e-03
10 20 30
....*....|....*....|....*....|....*...
gi 19111838 293 YAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNGA 330
Cdd:cd16021 178 YLNGLSLADEDLLEFLKRLKENGLLDNTFVIFMSDHGL 215
|
|
| |
