|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
44-460 |
4.71e-134 |
|
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: 397.26 E-value: 4.71e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGkegVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRKlQKMPM 123
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGNV---VKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS-RGFPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFPSYLRKAGYHTSNATKTDYNCFLDKTAWDVVE-------------GKIGEWRNRPDKRKPFFHVYTNAVTHEG 190
Cdd:cd16027 77 PDGVKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRgpddggrnawdyaSNAADFLNRAKKGQPFFLWFGFHDPHRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 191 KLQFKKNavkevPVHNNPASVTIHPYHPDTELFRYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLP 270
Cdd:cd16027 157 YPPGDGE-----EPGYDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGMPFP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 271 GTKGYTTEGGLQVPLVVYVPRKWreflpvKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFLGEDISLKQlNDRDE 350
Cdd:cd16027 232 RAKGTLYDSGLRVPLIVRWPGKI------KPGSVSDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKD-PGRDY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 351 VYGYGDRFDELYAFNRTVRKGRFKYSRNFQPyhskslyafyrykqaafrewkelyakgmlneiqkrffepqgaEELYDLS 430
Cdd:cd16027 305 VFAERDRHDETYDPIRSVRTGRYKYIRNYMP------------------------------------------EELYDLK 342
|
410 420 430
....*....|....*....|....*....|
gi 1782095189 431 VDPYETKNLATVPVYRSTLENLRILLKGKL 460
Cdd:cd16027 343 NDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
18-465 |
6.85e-81 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 260.58 E-value: 6.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 18 KRVGFIYAACCVTSsmsyAKEAPHERPNFVWFMAEDISKHYLSLYNDGKegVATPNVEKLAAEGIVFNNAYCNAPVSSAA 97
Cdd:COG3119 2 KRLLLLLLALLAAA----AAAAAAKRPNILFILADDLGYGDLGCYGNPL--IKTPNIDRLAAEGVRFTNAYVTSPVCSPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 98 RSTLITGCYAPRLGVSFHRKLQKMPMPEGLNMFPSYLRKAGYHTSNATK-----TDYncFLDKTAwdvvegkigEW-RNR 171
Cdd:COG3119 76 RASLLTGRYPHRTGVTDNGEGYNGGLPPDEPTLAELLKEAGYRTALFGKwhlylTDL--LTDKAI---------DFlERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 172 PDKRKPFFHVY-TNAVtHeGKLQFKKNAVKEVPVHNNPASVTIHPYHPDTELFRYTYATFYDRIQDSDTALGELIEMLKT 250
Cdd:COG3119 145 ADKDKPFFLYLaFNAP-H-APYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEELRRARAAYAAMIEEVDDQVGRLLDALEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 251 DGELDNTFVFYFGDNGGSLP-----GTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGIT 325
Cdd:COG3119 223 LGLADNTIVVFTSDNGPSLGehglrGGKGTLYEGGIRVPLIVRWPGK------IKAGSVSDALVSLIDLLPTLLDLAGVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 326 VPEGIDGTPFL----GEDIslkqlNDRDEVYGYGDRfdelYAFNRTVRKGRFKYSrnfqpyhskslyafyrykqaafrew 401
Cdd:COG3119 297 IPEDLDGRSLLplltGEKA-----EWRDYLYWEYPR----GGGNRAIRTGRWKLI------------------------- 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782095189 402 kelyakgmlneiqkRFFEPQGAEELYDLSVDPYETKNLATvpVYRSTLENLRILLKGKLLEEND 465
Cdd:COG3119 343 --------------RYYDDDGPWELYDLKNDPGETNNLAA--DYPEVVAELRALLEAWLKELGD 390
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
44-332 |
7.01e-56 |
|
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: 189.18 E-value: 7.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRKlQKMPM 123
Cdd:cd16022 1 PNILLIMTDDLGYDDLGCY--GNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVG-NGGGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFPSYLRKAGYHTSNATKTDyncflDKTAwdvvegkigEWRNRPDKRKPFFhVYTNavthegklqfkknavkevp 203
Cdd:cd16022 78 PPDEPTLAELLKEAGYRTALIGKWH-----DEAI---------DFIERRDKDKPFF-LYVS------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 204 vHNNPasvtiHpyHPdtelfrYTYATFYDRIqdsDTALGELIEMLKTDGELDNTFVFYFGDNGGSLP-----GTKGYTTE 278
Cdd:cd16022 124 -FNAP-----H--PP------FAYYAMVSAI---DDQIGRILDALEELGLLDNTLIVFTSDHGDMLGdhglrGKKGSLYE 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1782095189 279 GGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDG 332
Cdd:cd16022 187 GGIRVPFIVRWPGK------IPAGQVSDALVSLLDLLPTLLDLAGIEPPEGLDG 234
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
42-453 |
2.59e-50 |
|
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: 180.42 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFhrkLQKM 121
Cdd:cd16031 1 KRPNIIFILTDDHRYDALGCY--GNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTD---NNGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 122 PMPEGLNMFPSYLRKAGYHTSNATK--TDYNCFLDKTAWDVVEGKIG-------------------------------EW 168
Cdd:cd16031 76 LFDASQPTYPKLLRKAGYQTAFIGKwhLGSGGDLPPPGFDYWVSFPGqgsyydpefiengkrvgqkgyvtdiitdkalDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 169 RNRPDKRKPFF-------------------HVYTNAV----------THEGKLQFKKNAvkevpvHNNPASVTIHPYHPD 219
Cdd:cd16031 156 LKERDKDKPFClslsfkaphrpftpaprhrGLYEDVTipepetfdddDYAGRPEWAREQ------RNRIRGVLDGRFDTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 220 tELFRYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLpGTKGYTT-----EGGLQVPLVVYVPRKwr 294
Cdd:cd16031 230 -EKYQRYMKDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFL-GEHGLFDkrlmyEESIRVPLIIRDPRL-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 295 eflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDG---TPFLGEDislKQLNDRDEVYG--YGDRFDELYAFNRTVR 369
Cdd:cd16031 306 ----IKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGrslLPLLEGE---KPVDWRKEFYYeyYEEPNFHNVPTHEGVR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 370 KGRFKYSrnfqpyhskslyafyrykqaafrewkelyakgmlneiqkRFFEPQGAEELYDLSVDPYETKNLATVPVYRSTL 449
Cdd:cd16031 379 TERYKYI---------------------------------------YYYGVWDEEELYDLKKDPLELNNLANDPEYAEVL 419
|
....
gi 1782095189 450 ENLR 453
Cdd:cd16031 420 KELR 423
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-440 |
3.32e-43 |
|
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: 160.40 E-value: 3.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFH-------R 116
Cdd:cd16144 1 PNIVLILVDDLGWADLGCY--GSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQYPARLGITDVipgrrgpP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 117 KLQKMPMPEGLNMFPS-------YLRKAGYHT----------------------------SNATKTDYNCFLDKTAWDVV 161
Cdd:cd16144 79 DNTKLIPPPSTTRLPLeevtiaeALKDAGYATahfgkwhlggeggygpedqgfdvniggtGNGGPPSYYFPPGKPNPDLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 162 EGKIGEWRnrPD-------------KRKPFF-HVYTNAVtH-------EGKLQFKKNAVKEVPVHNNPasvtihpyhpdt 220
Cdd:cd16144 159 DGPEGEYL--TDrltdeaidfieqnKDKPFFlYLSHYAV-HtpiqarpELIEKYEKKKKGLRKGQKNP------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 221 elfryTYATFydrIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGG----------SLP--GTKGYTTEGGLQVPLVVY 288
Cdd:cd16144 224 -----VYAAM---IESLDESVGRILDALEELGLADNTLVIFTSDNGGlstrggpptsNAPlrGGKGSLYEGGIRVPLIVR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 289 VPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEG--IDGTPFL----GEDISLKqlndRDEVY----GYGDRF 358
Cdd:cd16144 296 WPGV------IKPGSVSDVPVIGTDLYPTFLELAGGPLPPPqhLDGVSLVpllkGGEADLP----RRALFwhfpHYHGQG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 359 DELYAfnrTVRKGRFKYsrnfqpyhskslyafyrykqaafrewkelyakgmlneIqkRFFEpQGAEELYDLSVDPYETKN 438
Cdd:cd16144 366 GRPAS---AIRKGDWKL-------------------------------------I--EFYE-DGRVELYNLKNDIGETNN 402
|
..
gi 1782095189 439 LA 440
Cdd:cd16144 403 LA 404
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
42-439 |
4.72e-43 |
|
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: 159.53 E-value: 4.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISkhylslYND----GKEgVATPNVEKLAAEGIVFNNAYcNAPVSSAARSTLITGCYAPRLGVSFhrk 117
Cdd:cd16025 1 GRPNILLILADDLG------FSDlgcfGGE-IPTPNLDALAAEGLRFTNFH-TTALCSPTRAALLTGRNHHQVGMGT--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 118 lqkmpMPEGLNMFPSY--------------LRKAGYHTS-----NATKTDYncFLDKtawDVVEgKIGEW-RNRPDKRKP 177
Cdd:cd16025 70 -----MAELATGKPGYegylpdsaatiaevLKDAGYHTYmsgkwHLGPDDY--YSTD---DLTD-KAIEYiDEQKAPDKP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 178 FFHVYTNAVTH-------------EGKlqFKK--NAVKE-----------VPvhnnpASVTIHPYHPDT----------- 220
Cdd:cd16025 139 FFLYLAFGAPHaplqapkewidkyKGK--YDAgwDALREerlerqkelglIP-----ADTKLTPRPPGVpawdslspeek 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 221 ELF-RY--TYATFYDRIqdsDTALGELIEMLKTDGELDNTFVFYFGDNGGS------------LPGTKGYTTEGGLQVPL 285
Cdd:cd16025 212 KLEaRRmeVYAAMVEHM---DQQIGRLIDYLKELGELDNTLIIFLSDNGASaepgwanasntpFRLYKQASHEGGIRTPL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 286 VVYVPRKWReflpvKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDG---TPFLGedISLKQL------NDRDEVYGYgd 356
Cdd:cd16025 289 IVSWPKGIK-----AKGGIRHQFAHVIDIAPTILELAGVEYPKTVNGvpqLPLDG--VSLLPTldgaaaPSRRRTQYF-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 357 rfdELYAfNRTVRKGRFKYSRNFQPYhskslyafyrykqAAFREWkelyakgmlneiqkrffepqgaeELYDLSVDPYET 436
Cdd:cd16025 360 ---ELFG-NRAIRKGGWKAVALHPPP-------------GWGDQW-----------------------ELYDLAKDPSET 399
|
...
gi 1782095189 437 KNL 439
Cdd:cd16025 400 HDL 402
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-440 |
2.05e-42 |
|
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: 157.73 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISkhylslYND----GKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRlgVSFHRKL 118
Cdd:cd16026 1 KPNIVVILADDLG------YGDlgcyGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPVR--VGLPGVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 119 QKMPMPEGLN----MFPSYLRKAGYHTSNATK---TDYNCFL----------------DKTAWDVVegkigewrnRPDKR 175
Cdd:cd16026 73 GPPGSKGGLPpdeiTIAEVLKKAGYRTALVGKwhlGHQPEFLptrhgfdeyfgipysnDMWPFPLY---------RNDPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 176 KPFFHVYTNAVTHEGK-------LQFKKNAVKEVPVH-NNP-----ASVTIH-PYHPDtELFRYTYA--TFYDRIQDSDT 239
Cdd:cd16026 144 GPLPPLMENEEVIEQPadqssltQRYTDEAVDFIERNkDQPfflylAHTMPHvPLFAS-EKFKGRSGagLYGDVVEELDW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 240 ALGELIEMLKTDGELDNTFVFYFGDNG---------GS---LPGTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDG 307
Cdd:cd16026 223 SVGRILDALKELGLEENTLVIFTSDNGpwleygghgGSagpLRGGKGTTWEGGVRVPFIAWWPGV------IPAGTVSDE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 308 FVSFMDLGPTLLHLAGITVPEG--IDG---TPFL-GEDISlkqlnDRDEVYGYGDRFDeLYAfnrtVRKGRFKysrnfqp 381
Cdd:cd16026 297 LASTMDLLPTLAALAGAPLPEDrvIDGkdiSPLLlGGSKS-----PPHPFFYYYDGGD-LQA----VRSGRWK------- 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1782095189 382 yhskslYAFYRYKQAAfrewkelyakgmlNEIQKRFFEPQGAEELYDLSVDPYETKNLA 440
Cdd:cd16026 360 ------LHLPTTYRTG-------------TDPGGLDPTKLEPPLLYDLEEDPGETYNVA 399
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-465 |
6.80e-42 |
|
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: 156.61 E-value: 6.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV--------SFH 115
Cdd:cd16033 1 PNILFIMTDQQRYDTLGCY--GNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVlnnvenagAYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 116 RKLqkmpmPEGLNMFPSYLRKAGYHT---------SNATKTDYNC--FLDKTA---WDVVEGKIGEWRNRPDKRKPFFhV 181
Cdd:cd16033 79 RGL-----PPGVETFSEDLREAGYRNgyvgkwhvgPEETPLDYGFdeYLPVETtieYFLADRAIEMLEELAADDKPFF-L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 182 YTN--------AVTHEGKLQFKKNAVKEvpvhnnPASV--TIH--PYHPDTELFRYTYATFYDRIQDS------------ 237
Cdd:cd16033 153 RVNfwgphdpyIPPEPYLDMYDPEDIPL------PESFadDFEdkPYIYRRERKRWGVDTEDEEDWKEiiahywgyitli 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 238 DTALGELIEMLKTDGELDNTFVFYFGDNGGSLPG----TKGYTT-EGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFM 312
Cdd:cd16033 227 DDAIGRILDALEELGLADDTLVIFTSDHGDALGAhrlwDKGPFMyEETYRIPLIIKWPGV------IAAGQVVDEFVSLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 313 DLGPTLLHLAGITVPEGIDGT---PFL-GEDISlkqlNDRDEVYG--YGdrfDELYAFNRTVRKGRFKYSrnfqpyhsks 386
Cdd:cd16033 301 DLAPTILDLAGVDVPPKVDGRsllPLLrGEQPE----DWRDEVVTeyNG---HEFYLPQRMVRTDRYKYV---------- 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782095189 387 lyafyrykqaafrewkelyakgmlneiqkrfFEPQGAEELYDLSVDPYETKNLATVPVYRSTLENLRILLKGKLLEEND 465
Cdd:cd16033 364 -------------------------------FNGFDIDELYDLESDPYELNNLIDDPEYEEILREMRTRLYEWMEETGD 411
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
42-457 |
1.70e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 154.64 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISkhYLSLYNDGKEGVATPNVEKLAAEGIVFNNAYC----NAPVSSAARSTLITGCY---APRLGvsf 114
Cdd:cd16155 1 KKPNILFILADDQR--ADTIGALGNPEIQTPNLDRLARRGTSFTNAYNmggwSGAVCVPSRAMLMTGRTlfhAPEGG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 115 hrklqKMPMPEGLNMFPSYLRKAGYHTSnATKTDYNCFLDKTawdvvegkIGEWRNRPDKRKPFF-HVYTNA--VTHEGK 191
Cdd:cd16155 76 -----KAAIPSDDKTWPETFKKAGYRTF-ATGKWHNGFADAA--------IEFLEEYKDGDKPFFmYVAFTAphDPRQAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 192 LQFKKN-AVKEVPVHNNPASVtiHPY--------------HPDTE------LFRYtYATfydrIQDSDTALGELIEMLKT 250
Cdd:cd16155 142 PEYLDMyPPETIPLPENFLPQ--HPFdngegtvrdeqlapFPRTPeavrqhLAEY-YAM----ITHLDAQIGRILDALEA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 251 DGELDNTFVFYFGDNGGSLpGTKG-------YttEGGLQVPLVVYVPrkwreflPVKVGQRVDGFVSFMDLGPTLLHLAG 323
Cdd:cd16155 215 SGELDNTIIVFTSDHGLAV-GSHGlmgkqnlY--EHSMRVPLIISGP-------GIPKGKRRDALVYLQDVFPTLCELAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 324 ITVPEGIDG---TPFLGEdislKQLNDRDEVYGYgdrfdelYAFN-RTVRKGRFKYsrnfqpyhskslyafyrykqaafr 399
Cdd:cd16155 285 IEIPESVEGkslLPVIRG----EKKAVRDTLYGA-------YRDGqRAIRDDRWKL------------------------ 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1782095189 400 ewkelyakgmlneiqKRFFEPQGAEELYDLSVDPYETKNLATVPVYRSTLENLRILLK 457
Cdd:cd16155 330 ---------------IIYVPGVKRTQLFDLKKDPDELNNLADEPEYQERLKKLLAELK 372
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-441 |
5.57e-40 |
|
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: 151.21 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV-SFHRKLQKMP 122
Cdd:cd16145 1 PNIIFILADDLGYGDLGCY--GQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVrGNSEPGGQDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 123 MPEGLNMFPSYLRKAGYHTSNATKTDYNCFLD-----KTAWDVVEGKIGE-----------WRNR---PDKRKPFFHVYT 183
Cdd:cd16145 79 LPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTpghptKQGFDYFYGYLDQvhahnyypeylWRNGekvPLPNNVIPPLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 184 NAVTHEGK------------LQF-KKNAVK---------------EVPV----HNNPASVTIHPYHPDTELFRyTYATFY 231
Cdd:cd16145 159 GNNAGGGGgtyshdlftdeaLDFiRENKDKpfflylaytlphaplQVPDdgpyKYKPKDPGIYAYLPWPQPEK-AYAAMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 232 DRIqdsDTALGELIEMLKTDGELDNTFVFYFGDNG-----------------GSLPGTKGYTTEGGLQVPLVVYVPRKwr 294
Cdd:cd16145 238 TRL---DRDVGRILALLKELGIDENTLVVFTSDNGphseggsehdpdffdsnGPLRGYKRSLYEGGIRVPFIARWPGK-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 295 eflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFLGEdislkqLNDRDEvygyGDRFDELYafnrtvrkgrfk 374
Cdd:cd16145 313 ----IPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPT------LLGKPQ----QQQHDYLY------------ 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 375 ysrnfqpyhskslYAFY--RYKQAAFR-EWKELyakgmlneiqkRFFEPQGAEELYDLSVDPYETKNLAT 441
Cdd:cd16145 367 -------------WEFYegGGAQAVRMgGWKAV-----------RHGKKDGPFELYDLSTDPGETNNLAA 412
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
44-324 |
1.13e-39 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGKEgvATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRKLQKMPM 123
Cdd:pfam00884 1 PNVVLVLGESLRAPDLGLYGYPRP--TTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPVGLPRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLnmfPSYLRKAGYHTSNATKTDYNcFLDKTAwdVVEGKIGEWRNRPDKRKPFFHVYTNAVTHEGKL----QFKKNAV 199
Cdd:pfam00884 79 EPSL---PDLLKRAGYNTGAIGKWHLG-WYNNQS--PCNLGFDKFFGRNTGSDLYADPPDVPYNCSGGGvsdeALLDEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 200 KEVPVHNNPASVTIHPYHPDTELF---RY--TYATFYDRIQD--------------SDTALGELIEMLKTDGELDNTFVF 260
Cdd:pfam00884 153 EFLDNNDKPFFLVLHTLGSHGPPYypdRYpeKYATFKPSSCSeeqllnsydntllyTDDAIGRVLDKLEENGLLDNTLVV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782095189 261 YFGDNGGSLPGTKGY--------TTEGGLQVPLVVYVPRKWREflpvkvGQRVDGFVSFMDLGPTLLHLAGI 324
Cdd:pfam00884 233 YTSDHGESLGEGGGYlhggkydnAPEGGYRVPLLIWSPGGKAK------GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-386 |
4.07e-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: 293770 [Multi-domain] Cd Length: 377 Bit Score: 142.35 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNaPVSSAARSTLITGCYAPRLGVSFHRKLQKMPm 123
Cdd:cd16151 1 PNIILIMADDLGYECIGCY--GGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNYVVFGYLDPKQK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 peglnMFPSYLRKAGYHTSNATK---TDYNCFLDKTA---------WDVVEGKIGEWRNRPdkrkPFFHVYTNAVTHEGK 191
Cdd:cd16151 77 -----TFGHLLKDAGYATAIAGKwqlGGGRGDGDYPHefgfdeyclWQLTETGEKYSRPAT----PTFNIRNGKLLETTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 192 LQF-------------KKNavKEVP---------VHnNPASVTIHPYHPDTELFRYT--YATFYDRIQDSDTALGELIEM 247
Cdd:cd16151 148 GDYgpdlfadflidfiERN--KDQPffayypmvlVH-DPFVPTPDSPDWDPDDKRKKddPEYFPDMVAYMDKLVGKLVDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 248 LKTDGELDNTFVFYFGDNG-----------GSLPGTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGP 316
Cdd:cd16151 225 LEELGLRENTIIIFTGDNGthrpitsrtngREVRGGKGKTTDAGTHVPLIVNWPGL------IPAGGVSDDLVDFSDFLP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782095189 317 TLLHLAGITVPEG--IDGTPFLgEDISLKQLNDRDEVYGYGDRFDELYAFNRTVRKGRFKYSRNFQPYHSKS 386
Cdd:cd16151 299 TLAELAGAPLPEDypLDGRSFA-PQLLGKTGSPRREWIYWYYRNPHKKFGSRFVRTKRYKLYADGRFFDLRE 369
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
42-445 |
4.64e-37 |
|
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: 143.48 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDIsKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV----SFHRK 117
Cdd:cd16030 1 KKPNVLFIAVDDL-RPWLGCY--GGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVydnnSYFRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 118 LqkmpMPEGLNMfPSYLRKAGYHTSNATKT----DYNCFLDKTAWDVV-------------------------------- 161
Cdd:cd16030 78 V----APDAVTL-PQYFKENGYTTAGVGKIfhpgIPDGDDDPASWDEPpnppgpekyppgklcpgkkggkgggggpawea 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 162 ---------EGKIGEW-----RNRPDKRKPFF--------HvytnavthegkLQF---KK------NAVKEVPVHNNPAS 210
Cdd:cd16030 153 advpdeaypDGKVADEaieqlRKLKDSDKPFFlavgfykpH-----------LPFvapKKyfdlypLESIPLPNPFDPID 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 211 VTIHPYHPDTELFRYT-----YATFYDRIQDSDTA-----------------LGELIEMLKTDGELDNTFVFYFGDNGGS 268
Cdd:cd16030 222 LPEVAWNDLDDLPKYGdipalNPGDPKGPLPDEQArelrqayyasvsyvdaqVGRVLDALEELGLADNTIVVLWSDHGWH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 269 LpGTKG----YTT-EGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTpflgediSLK 343
Cdd:cd16030 302 L-GEHGhwgkHTLfEEATRVPLIIRAPGV------TKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGK-------SLV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 344 -QLND-----RDEVYGygdRFDELYAFNRTVRKGRFKYSrnfqpyhskslyafyrykqaafrEWKElyakgmlneiqkrf 417
Cdd:cd16030 368 pLLKNpsakwKDAAFS---QYPRPSIMGYSIRTERYRYT-----------------------EWVD-------------- 407
|
490 500
....*....|....*....|....*...
gi 1782095189 418 FEPQGAEELYDLSVDPYETKNLATVPVY 445
Cdd:cd16030 408 FDKVGAEELYDHKNDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-453 |
1.20e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 139.29 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAE----DISKHYlslyndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGvsfHRKLQ 119
Cdd:cd16150 1 PNIVIFVADqlraDSLGHL------GNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG---HRTLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 120 KMPMPEGLNMFpSYLRKAGYHTSNATKTDY---NCFLDKTA---WDVVEGKIgEWRNRPDKRKPFF--------HV---- 181
Cdd:cd16150 72 HLLRPDEPNLL-KTLKDAGYHVAWAGKNDDlpgEFAAEAYCdsdEACVRTAI-DWLRNRRPDKPFClylplifpHPpygv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 182 ---YTNAVTHEGKLQfkknAVKEVPVHNNPASVTIHP-YHPDTEL----FRYTYATFYDRIQDSDTALGELIEMLKTDGE 253
Cdd:cd16150 150 eepWFSMIDREKLPP----RRPPGLRAKGKPSMLEGIeKQGLDRWseerWRELRATYLGMVSRLDHQFGRLLEALKETGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 254 LDNTFVFYFGDNGgslpgtkGYTTEGGL-------------QVPLVVYVPrkwreflPVKVGQRVDGFVSFMDLGPTLLH 320
Cdd:cd16150 226 YDDTAVFFFSDHG-------DYTGDYGLvekwpntfedcltRVPLIIKPP-------GGPAGGVSDALVELVDIPPTLLD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 321 LAGITVPEGIDGTPFL----GEDISLkqlndRDEVYGYGDR-FDELYAFNRTVRKGRFKYSRNFQ----PYHSKslyafy 391
Cdd:cd16150 292 LAGIPLSHTHFGRSLLpvlaGETEEH-----RDAVFSEGGRlHGEEQAMEGGHGPYDLKWPRLLQqeepPEHTK------ 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782095189 392 rykqaAF----REWKELYakgmlneiqkRFFEPqgaEELYDLSVDPYETKNLATVPVYRSTLENLR 453
Cdd:cd16150 361 -----AVmirtRRYKYVY----------RLYEP---DELYDLEADPLELHNLIGDPAYAEIIAEMK 408
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-334 |
1.50e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 135.20 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLYN-------DGKEG-VATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV-S 113
Cdd:cd16153 1 KPNILWIITDDQRVDSLSCYNnahtgksESRLGyVESPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 114 FHRKLQKmpMPEGLNMFPSYLRKAGYHTSNATKTDYNCFLD--KTAWDVVEGKIGEWRNRPDKRKPFFhvytnavTHEGK 191
Cdd:cd16153 81 FEAAHPA--LDHGLPTFPEVLKKAGYQTASFGKSHLEAFQRylKNANQSYKSFWGKIAKGADSDKPFF-------VRLSF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 192 LQfkknavkevpvhnnPASVTIHPyHPDTELFRYTYATFYdriqdSDTALGELIEMLKTDGEL---DNTFVFYFGDNGGS 268
Cdd:cd16153 152 LQ--------------PHTPVLPP-KEFRDRFDYYAFCAY-----GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWH 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782095189 269 LpGTKGYTTEGG-----LQVPLVVYVPRKwrefLPVKVGQRVDGFVSFMDLGPTLLHLAGITV--PEGIDGTP 334
Cdd:cd16153 212 L-GEQGILAKFTfwpqsHRVPLIVVSSDK----LKAPAGKVRHDFVEFVDLAPTLLAAAGVDVdaPDYLDGRD 279
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-375 |
3.90e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 135.36 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRklqkMPM 123
Cdd:cd16037 1 PNILIIMSDEHNPDAMGCY--GHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNA----DPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFPSYLRKAGYHTSNATKTDYNCFLDKTAW----DVVEGKIGEWRNRPDKRKPFFHVytnavthegklqfkknaV 199
Cdd:cd16037 75 DGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHGFrydrDVTEAAVDWLREEAADDKPWFLF-----------------V 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 200 KEVPVHnnpasvtiHPYHPDTELFRYtY-----ATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLpGTKG 274
Cdd:cd16037 138 GFVAPH--------FPLIAPQEFYDL-YvrrarAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDML-GERG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 275 -------YttEGGLQVPLVVYVPRkwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGtpflgedISLKQLND 347
Cdd:cd16037 208 lwgkstmY--EESVRVPMIISGPG-------IPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDG-------RSLLPLAE 271
|
330 340 350
....*....|....*....|....*....|....*
gi 1782095189 348 RDEVYgygDR--FDELYAFNRT-----VRKGRFKY 375
Cdd:cd16037 272 GPDDP---DRvvFSEYHAHGSPsgafmLRKGRWKY 303
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
43-439 |
9.89e-35 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 136.16 E-value: 9.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVsFHrklQKMP 122
Cdd:cd16034 1 KPNILFIFADQHRAQALGCA--GDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGV-FG---NDVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 123 MPEGLNMFPSYLRKAGYHTS------------------NAT-----------KTDYNCF---LDKTAW--DVVEGKIGEW 168
Cdd:cd16034 75 LPPDAPTIADVLKDAGYRTGyigkwhldgperndgradDYTppperrhgfdyWKGYECNhdhNNPHYYddDGKRIYIKGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 169 -------------RNRPDKRKPFFHV---------YTNAVThEGKLQFKKnavKEVPVHNNpasvtIHPYHPDTELFRYT 226
Cdd:cd16034 155 spdaetdlaieylENQADKDKPFALVlswnpphdpYTTAPE-EYLDMYDP---KKLLLRPN-----VPEDKKEEAGLRED 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 227 YATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNG---GS--LPGtKGYTTEGGLQVPLVVYVPRKwreflpVKV 301
Cdd:cd16034 226 LRGYYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGShgLMN-KQVPYEESIRVPFIIRYPGK------IKA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 302 GQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTpflgeDISLKQLNDRDE-----VYGYGDRFDELYAFN----RTVRKGR 372
Cdd:cd16034 299 GRVVDLLINTVDIMPTLLGLCGLPIPDTVEGR-----DLSPLLLGGKDDepdsvLLQCFVPFGGGSARDggewRGVRTDR 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782095189 373 FKYSRNfqpyhskslyafyrykqaafrEWKELYakgmlneiqkrffepqgaeeLYDLSVDPYETKNL 439
Cdd:cd16034 374 YTYVRD---------------------KNGPWL--------------------LFDNEKDPYQLNNL 399
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
71-453 |
4.20e-34 |
|
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: 133.51 E-value: 4.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 71 TPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVsFHRKLqkmPMPEGLNMFPSYLRKAGYHTsnatktdyn 150
Cdd:cd16152 27 TPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGC-FRNGI---PLPADEKTLAHYFRDAGYET--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 151 cfldktawdvveGKIGEW------------------RNRpDKRKPFF--------HVYTNAVTHEGKLQFK-KNAVKEVP 203
Cdd:cd16152 94 ------------GYVGKWhlagyrvdaltdfaidylDNR-QKDKPFFlflsylepHHQNDRDRYVAPEGSAeRFANFWVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 204 vhnnpasvtihpyhPDTELF----RYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGG---SLPGT-KGY 275
Cdd:cd16152 161 --------------PDLAALpgdwAEELPDYLGCCERLDENVGRIRDALKELGLYDNTIIVFTSDHGChfrTRNAEyKRS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 276 TTEGGLQVPLVVYVPrkwreflPVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFLgEDISLKQLNDRDEVY--- 352
Cdd:cd16152 227 CHESSIRVPLVIYGP-------GFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLL-PLVDGKVEDWRNEVFiqi 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 353 -----GygdrfdelyafnRTVRKGRFKYSRnFQPYHSKslyafyrykqaafreWKELYAkgmlneiqKRFFEpqgaEELY 427
Cdd:cd16152 299 sesqvG------------RAIRTDRWKYSV-AAPDKDG---------------WKDSGS--------DVYVE----DYLY 338
|
410 420
....*....|....*....|....*.
gi 1782095189 428 DLSVDPYETKNLATVPVYRSTLENLR 453
Cdd:cd16152 339 DLEADPYELVNLIGRPEYREVAAELR 364
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-336 |
3.49e-33 |
|
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: 128.43 E-value: 3.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSfhrklqKMPM 123
Cdd:cd16148 1 MNVILIVIDSLRADHLGCY--GYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW------GGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFPSYLRKAGYHT---SNATKTDYNCFLDKT--AWDVVEGKIG------------------EWRNRPDKRKPFF- 179
Cdd:cd16148 73 EPDDPTLAEILRKAGYYTaavSSNPHLFGGPGFDRGfdTFEDFRGQEGdpgeegderaervtdralEWLDRNADDDPFFl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 180 HVYTNAvTHEgklqfkknavkevpvhnnpasvtihPYHPDTELfRYTyatfydriqdsDTALGELIEMLKTDGELDNTFV 259
Cdd:cd16148 153 FLHYFD-PHE-------------------------PYLYDAEV-RYV-----------DEQIGRLLDKLKELGLLEDTLV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 260 -------FYFGDNGgslpgtkGYTTEGG------LQVPLVVYVPRKWReflpvkvGQRVDGFVSFMDLGPTLLHLAGITV 326
Cdd:cd16148 195 ivtsdhgEEFGEHG-------LYWGHGSnlydeqLHVPLIIRWPGKEP-------GKRVDALVSHIDIAPTLLDLLGVEP 260
|
330
....*....|
gi 1782095189 327 PEGIDGTPFL 336
Cdd:cd16148 261 PDYSDGRSLL 270
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
44-375 |
8.40e-33 |
|
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: 128.85 E-value: 8.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV----Sfhrklq 119
Cdd:cd16032 1 PNILLIMADQLTAAALPAY--GNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAydnaA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 120 kmPMPEGLNMFPSYLRKAGYHTSNATKT-----------DYNcflDKTAWDVVEgKIGEWRNRPDKRkPFFhvYTNAVTH 188
Cdd:cd16032 73 --EFPADIPTFAHYLRAAGYRTALSGKMhfvgpdqlhgfDYD---EEVAFKAVQ-KLYDLARGEDGR-PFF--LTVSFTH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 189 egklqfkknavkevPvHNnpasvtihPYHPDTELF-RYTYAT---FYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGD 264
Cdd:cd16032 144 --------------P-HD--------PYVIPQEYWdLYVRRArraYYGMVSYVDDKVGQLLDTLERTGLADDTIVIFTSD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 265 NGGSLpGTKG-------YttEGGLQVPLVVYVPRKWReflpvkvGQRVDGFVSFMDLGPTLLHLAGITVPEG---IDG-- 332
Cdd:cd16032 201 HGDML-GERGlwykmsfF--EGSARVPLIISAPGRFA-------PRRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDGrs 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1782095189 333 -TPFLGEDislkQLNDRDEVygYGDRFDE-LYAFNRTVRKGRFKY 375
Cdd:cd16032 271 lLPLLEGG----DSGGEDEV--ISEYLAEgAVAPCVMIRRGRWKF 309
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-440 |
1.15e-32 |
|
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: 129.58 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGKE-GVATPNVEKLAAEGIVFNNAYCNaPVSSAARSTLITGCYAPRLGvsfhrkLQKMP 122
Cdd:cd16142 1 PNILVILGDDIGWGDLGCYGGGIGrGAPTPNIDRLAKEGLRFTSFYVE-PSCTPGRAAFITGRHPIRTG------LTTVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 123 MP-EGLNM------FPSYLRKAGYHTSNATK-----------TD-----YNCFLDKTAWDVVEGKIGEW--RNRPDKrKP 177
Cdd:cd16142 74 LPgSPGGLppweptLAELLKDAGYATAQFGKwhlgdedgrlpTDhgfdeFYGNLYHTIDEEIVDKAIDFikRNAKAD-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 178 FFhVYTNAVThegklqfkknavkevpVHnnpasVTIHPyHPDtelFR------YTYAtfyDRIQDSDTALGELIEMLKTD 251
Cdd:cd16142 153 FF-LYVNFTK----------------MH-----FPTLP-SPE---FEgkssgkGKYA---DSMVELDDHVGQILDALDEL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 252 GELDNTFVFYFGDNG---------GSLP--GTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLH 320
Cdd:cd16142 204 GIADNTIVIFTTDNGpeqdvwpdgGYTPfrGEKGTTWEGGVRVPAIVRWPGK------IKPGRVSNEIVSHLDWFPTLAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 321 LAGITVPE-----------GIDGTPFL-GEDislkQLNDRDEVYGYGDrfDELYAfnrtVRKGRFKysrnfqpYHSKsly 388
Cdd:cd16142 278 LAGAPDPKdkllgkdrhidGVDQSPFLlGKS----EKSRRSEFFYFGE--GELGA----VRWKNWK-------VHFK--- 337
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1782095189 389 afyrykqaafreWKELYAKGMLNEiqkrfFEPQGAEELYDLSVDPYETKNLA 440
Cdd:cd16142 338 ------------AQEDTGGPTGEP-----FYVLTFPLIFNLRRDPKERYDVT 372
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
44-440 |
8.04e-32 |
|
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: 127.70 E-value: 8.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISkhY--LSLYNDgKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRL----GVSFHrk 117
Cdd:cd16143 1 PNIVIILADDLG--YgdISCYNP-DSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSrlkgGVLGG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 118 LQKMPMPEGLNMFPSYLRKAGYHTSnatktdynCF------LDktaWDVVEGK--IGEWRNRPDKRKP------------ 177
Cdd:cd16143 76 FSPPLIEPDRVTLAKMLKQAGYRTA--------MVgkwhlgLD---WKKKDGKkaATGTGKDVDYSKPikggpldhgfdy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 178 FFHVYTNAV---THEGKLQFKKNAVKEvpvhNNP-----ASVTIH-PYHPDTELFRYTYATFY-DRIQDSDTALGELIEM 247
Cdd:cd16143 145 YFGIPASEVlptLTDKAVEFIDQHAKK----DKPfflyfALPAPHtPIVPSPEFQGKSGAGPYgDFVYELDWVVGRILDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 248 LKTDGELDNTFVFYFGDNGGSLP------------------GTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFV 309
Cdd:cd16143 221 LKELGLAENTLVIFTSDNGPSPYadykelekfghdpsgplrGMKADIYEGGHRVPFIVRWPGK------IPAGSVSDQLV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 310 SFMDLGPTLLHLAGITVP--EGIDGTPFLGEDISLKQLNDRDEVYgYGDRFDELyafnrTVRKGrfkysrnfqpyhsksl 387
Cdd:cd16143 295 SLTDLFATLAAIVGQKLPdnAAEDSFSFLPALLGPKKQEVRESLV-HHSGNGSF-----AIRKG---------------- 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1782095189 388 yafyrykqaafrEWKELYAKGMLNEIQKRFFEPQGAE--ELYDLSVDPYETKNLA 440
Cdd:cd16143 353 ------------DWKLIDGTGSGGFSYPRGKEKLGLPpgQLYNLSTDPGESNNLY 395
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
42-468 |
1.18e-28 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 119.77 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISKHYLSLynDGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGcYAP----RLG----VS 113
Cdd:PRK13759 5 KKPNIILIMVDQMRGDCLGC--NGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTG-LSQwhhgRVGygdvVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 114 FHRKlqkmpmpeglNMFPSYLRKAGYHTS--------------------------------------------------- 142
Cdd:PRK13759 82 WNYK----------NTLPQEFRDAGYYTQcigkmhvfpqrnllgfhnvllhdgylhsgrnedksqfdfvsdylawlreka 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 143 ---NATKTD--YNCF------------LDKTAWdVVEGKIgEWRNRPDKRKPFFHVYTNAVTH------EGKLQFKKNA- 198
Cdd:PRK13759 152 pgkDPDLTDigWDCNswvarpwdleerLHPTNW-VGSESI-EFLRRRDPTKPFFLKMSFARPHspydppKRYFDMYKDAd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 199 VKEVPVHNNPASVTIHP--YHPDT-------ELFRYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSL 269
Cdd:PRK13759 230 IPDPHIGDWEYAEDQDPegGSIDAlrgnlgeEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGDML 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 270 pGT-----KGYTTEGGLQVPLVVYVPRKwreFLPVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFLgEDISLKQ 344
Cdd:PRK13759 310 -GDhylfrKGYPYEGSAHIPFIIYDPGG---LLAGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLK-NLIFGQY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 345 LNDRDEVYGygdrfdE---LYAFNRTVRKGRFKYSRNFQpyhskslyafyrykqaafrewkelyakgmlneiqkrffepQ 421
Cdd:PRK13759 385 EGWRPYLHG------EhalGYSSDNYLTDGKWKYIWFSQ----------------------------------------T 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1782095189 422 GAEELYDLSVDPYETKNLATVPVYRSTLENLRILLKGKlLEENDLGF 468
Cdd:PRK13759 419 GEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVDH-LRGREEGF 464
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-331 |
7.99e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 112.72 E-value: 7.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV-----SFHRKL 118
Cdd:cd16149 1 PNILFILTDDQGPWALGCY--GNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 119 QKMPMP--EGLNMFPSYLRKAGYHTSNATK----TDYNCFLDKtawdvvegkigewrnRPDKRKPFFhvytnavthegkL 192
Cdd:cd16149 79 TKKPEGylEGQTTLPEVLQDAGYRCGLSGKwhlgDDAADFLRR---------------RAEAEKPFF------------L 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 193 QFKKNAvkevpvhnnpasvtihPYHPdtelFRYtYATfydrIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLpGT 272
Cdd:cd16149 132 SVNYTA----------------PHSP----WGY-FAA----VTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNM-GH 185
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 273 -----KGYTT------EGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGID 331
Cdd:cd16149 186 hgiwgKGNGTfplnmyDNSVKVPFIIRWPGV------VPAGRVVDSLVSAYDFFPTLLELAGVDPPADPR 249
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
71-440 |
1.22e-27 |
|
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: 115.72 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 71 TPNVEKLAAEGIVFNNAYcNAPVSSAARSTLITGCYAPRLGVsFHRKLQKMPMPEGLNMFPSYLRKAGYHTsnatktdyn 150
Cdd:cd16146 26 TPNLDRLAAESVRFTNFH-VSPVCAPTRAALLTGRYPFRTGV-WHTILGRERMRLDETTLAEVFKDAGYRT--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 151 cfldktawdvveGKIGEWRN------RPDKR----------------------KPFFHVYTN---AVTHEG--------- 190
Cdd:cd16146 95 ------------GIFGKWHLgdnypyRPQDRgfdevlghggggigqypdywgnDYFDDTYYHngkFVKTEGyctdvffde 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 191 KLQF-KKNavKEVPV-----HNNPasvtiH-PYH-PDTELFRY-------TYATFYDRIQDSDTALGELIEMLKTDGELD 255
Cdd:cd16146 163 AIDFiEEN--KDKPFfaylaTNAP-----HgPLQvPDKYLDPYkdmglddKLAAFYGMIENIDDNVGRLLAKLKELGLEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 256 NTFVFYFGDNGGSLP----------GTKGYTTEGGLQVPLVVYVPRKWreflpvKVGQRVDGFVSFMDLGPTLLHLAGIT 325
Cdd:cd16146 236 NTIVIFMSDNGPAGGvpkrfnagmrGKKGSVYEGGHRVPFFIRWPGKI------LAGKDVDTLTAHIDLLPTLLDLCGVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 326 VPEG--IDGTPFLGEdisLKQ----LNDRDEVYGYGDRFDELYAFNRT-VRKGRFKYSRNfqpyhskslyafyrykqaaf 398
Cdd:cd16146 310 LPEGikLDGRSLLPL---LKGesdpWPERTLFTHSGRWPPPPKKKRNAaVRTGRWRLVSP-------------------- 366
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1782095189 399 rewkelyakgmlneiqkrffePQGAEELYDLSVDPYETKNLA 440
Cdd:cd16146 367 ---------------------KGFQPELYDIENDPGEENDVA 387
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
44-462 |
2.82e-27 |
|
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: 115.05 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYaprlgVSFHRKLQ-KMP 122
Cdd:cd16028 1 RNVLFITADQWRADCLSCL--GHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRY-----LMNHRSVWnGTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 123 MPEGLNMFPSYLRKAGYHTSNATKTDY--------------------------NCFLD-------KTAWdVVEGKIGEWR 169
Cdd:cd16028 74 LDARHLTLALELRKAGYDPALFGYTDTspdprglapldprllsyelampgfdpVDRLDeypaedsDTAF-LTDRAIEYLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 170 NRPDKR-----------------KPFFHVYTNAvthegklqfkknavkEVP----VHNNPASVTIHPY------HPDTEL 222
Cdd:cd16028 153 ERQDEPwflhlsyirphppfvapAPYHALYDPA---------------DVPppirAESLAAEAAQHPLlaafleRIESLS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 223 FRYTY---------------ATFYDRIQDSDTALGELIEMLKTDGELDNTF-VF------YFGDNGgsLPGTKGYTtEGG 280
Cdd:cd16028 218 FSPGAanaadlddeevaqmrATYLGLIAEVDDHLGRLFDYLKETGQWDDTLiVFtsdhgeQLGDHW--LWGKDGFF-DQA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 281 LQVPLVVYVPRKWREflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDG---TPFL-GEDISLKqlndRDEVYgYGD 356
Cdd:cd16028 295 YRVPLIVRDPRREAD---ATRGQVVDAFTESVDVMPTILDWLGGEIPHQCDGrslLPLLaGAQPSDW----RDAVH-YEY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 357 RFDELY------AFNRT--------VRKGRFKYsrnfqpYHskslyaFyrykqAAFRewkelyakgmlneiqkrffePQg 422
Cdd:cd16028 367 DFRDVStrrpqeALGLSpdecslavIRDERWKY------VH------F-----AALP--------------------PL- 408
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1782095189 423 aeeLYDLSVDPYETKNLATVPVYRSTLENLRillkGKLLE 462
Cdd:cd16028 409 ---LFDLKNDPGELRDLAADPAYAAVVLRYA----QKLLS 441
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-381 |
1.77e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 109.99 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDisKHYLSLYNDGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPrlgvsfhrkLQKMPM 123
Cdd:cd16035 1 PNILLILTDQ--ERYPPPWPAGWAALNLPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQ---------QTGVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFP----------SYLRKAGYHT--------SNATKTDYNcFLDKTAWDVVEGkIGEWRNRPDKRKPFFHVyTNA 185
Cdd:cd16035 70 TLGSPMQPllspdvptlgHMLRAAGYYTaykgkwhlSGAAGGGYK-RDPGIAAQAVEW-LRERGAKNADGKPWFLV-VSL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 186 VthegklqfkknavkevpvhnNPASVTihpYHPDTELFRYTYATFYDR-IQDSDTALGELIEMLKTDGELDNTFVFYFGD 264
Cdd:cd16035 147 V--------------------NPHDIM---FPPDDEERWRRFRNFYYNlIRDVDRQIGRVLDALDASGLADNTIVVFTSD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 265 NG---GSLPGT-KGYTT-EGGLQVPLVVYVPRKWreflpvKVGQRVDGFVSFMDLGPTLLHLAGITVPE-GIDGTPFLGE 338
Cdd:cd16035 204 HGemgGAHGLRgKGFNAyEEALHVPLIISHPDLF------GTGQTTDALTSHIDLLPTLLGLAGVDAEArATEAPPLPGR 277
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1782095189 339 DISlKQLNDRDevygyGDRFDELYAFNRTvrkgRFKYSRNFQP 381
Cdd:cd16035 278 DLS-PLLTDAD-----ADAVRDGILFTYD----RYKFARYFDP 310
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
43-440 |
4.14e-25 |
|
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: 108.02 E-value: 4.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLyndgkeGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV--------SF 114
Cdd:cd16147 1 RPNIVLILTDDQDVELGSM------DPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVtnnsppggGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 115 HRKLQKMPMPeglNMFPSYLRKAGYHT------------------------------SNATKTDYNCFLDK--------- 155
Cdd:cd16147 75 PKFWQNGLER---STLPVWLQEAGYRTayagkylngygvpggvsyvppgwdewdglvGNSTYYNYTLSNGGngkhgvsyp 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 156 ----TawDVVEGKIGEW-RNRPDKRKPFF--------HV-YTNAVTHEGKLQFKKNA----VKEVPVHNNPASVTIHPYH 217
Cdd:cd16147 152 gdylT--DVIANKALDFlRRAAADDKPFFlvvappapHGpFTPAPRYANLFPNVTAPprppPNNPDVSDKPHWLRRLPPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 218 PDTELfRYTYATFYDRIQDS---DTALGELIEMLKTDGELDNTFVFYFGDNG---G--SLPGTK--GYTTEggLQVPLVV 287
Cdd:cd16147 230 NPTQI-AYIDELYRKRLRTLqsvDDLVERLVNTLEATGQLDNTYIIYTSDNGyhlGqhRLPPGKrtPYEED--IRVPLLV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 288 YVPRkwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPflgedislkqlndrdevygygdrfdELYAFNRT 367
Cdd:cd16147 307 RGPG-------IPAGVTVDQLVSNIDLAPTILDLAGAPPPSDMDGRS-------------------------CGDSNNNT 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782095189 368 vrkgrFKYSRNFQPYHSKSLYafyrykqaafrEWKElyakgmlneiqkrffepqGAEELYDLSVDPYETKNLA 440
Cdd:cd16147 355 -----YKCVRTVDDTYNLLYF-----------EWCT------------------GFRELYDLTTDPYQLTNLA 393
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
42-356 |
6.58e-25 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 109.36 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISKHYLSLYNDGKEgvATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRKLQKm 121
Cdd:COG1368 233 KKPNVVVILLESFSDFFIGALGNGKD--VTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPLPGGSPYKRPGQN- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 122 pmpeGLNMFPSYLRKAGYHTS---NATKTDYNC-----------FLDKTAWDVVEgkIGEW------------RNRPDKR 175
Cdd:COG1368 310 ----NFPSLPSILKKQGYETSffhGGDGSFWNRdsfyknlgfdeFYDREDFDDPF--DGGWgvsdedlfdkalEELEKLK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 176 KPFFHVYTNAVTHegklqfkknavkevpvhnnpasvtiHPYHPDTELFRY------TYATFYDRIQDSDTALGELIEMLK 249
Cdd:COG1368 384 KPFFAFLITLSNH-------------------------GPYTLPEEDKKIpdygktTLNNYLNAVRYADQALGEFIEKLK 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 250 TDGELDNT-FVFYfGDNGGSLPGTKGYTTEGGLQ-VPLVVYVPrkwreflPVKVGQRVDGFVSFMDLGPTLLHLAGITVP 327
Cdd:COG1368 439 KSGWYDNTiFVIY-GDHGPRSPGKTDYENPLERYrVPLLIYSP-------GLKKPKVIDTVGSQIDIAPTLLDLLGIDYP 510
|
330 340
....*....|....*....|....*....
gi 1782095189 328 EgidgTPFLGEDIslkqLNDRDEVYGYGD 356
Cdd:COG1368 511 S----YYAFGRDL----LSPDTDPFAFRN 531
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
44-440 |
1.05e-24 |
|
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: 106.48 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISkhylslYND----GKEGVATPNVEKLAAEGIVFNNAYcNAPVSSAARSTLITGCYAPRLGVSfHRKLQ 119
Cdd:cd16029 1 PHIVFILADDLG------WNDvgfhGSDQIKTPNLDALAADGVILNNYY-VQPICTPSRAALMTGRYPIHTGMQ-HGVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 120 KmPMPEGLN----MFPSYLRKAGYHTSNATK---------------------------TDYNCFLDKTAWDVveGKIGEW 168
Cdd:cd16029 73 A-GEPYGLPlnetLLPQYLKELGYATHLVGKwhlgfytweytptnrgfdsfygyyggaEDYYTHTSGGANDY--GNDDLR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 169 RNRpdkrKPFFHVYTNAVTHegklQFKKNAVKEVPVHN--NP-----ASVTIHPYHPDTELFRYTYATFYDRIQDS---- 237
Cdd:cd16029 150 DNE----EPAWDYNGTYSTD----LFTDRAVDIIENHDpsKPlflylAFQAVHAPLQVPPEYADPYEDKFAHIKDEdrrt 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 238 --------DTALGELIEMLKTDGELDNTFVFYFGDNGGS-----------LPGTKGYTTEGGLQVPLVVYVPrkwreFLP 298
Cdd:cd16029 222 yaamvsalDESVGNVVDALKAKGMLDNTLIVFTSDNGGPtgggdggsnypLRGGKNTLWEGGVRVPAFVWSP-----LLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 299 VKVGQRVDGFVSFMDLGPTLLHLAGITVPegiDGTPFLGEDI--SLKQLND--RDEV-YGYgdrfDELYAFNRT--VRKG 371
Cdd:cd16029 297 PKRGTVSDGLMHVTDWLPTLLSLAGGDPD---DLPPLDGVDQwdALSGGAPspRTEIlLNI----DDITRTTGGaaIRVG 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782095189 372 RFKYSRNFQpyhskslyafyrykqaafrewkelyakgmlneiqkrffepqgaeeLYDLSVDPYETKNLA 440
Cdd:cd16029 370 DWKLIVGKP---------------------------------------------LFNIENDPCERNDLA 393
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
43-439 |
7.46e-24 |
|
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: 104.09 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLyNDGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV--SFH-RKLQ 119
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGA-NWAPNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMTGRLGLRNGVghNFLpTSVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 120 KMPMPEglNMFPSYLRKAGYHTsnatktdyncfldktawdvveGKIGEW------RNRPDKRKpFFHVYTNAVTHEGKLQ 193
Cdd:cd16161 80 GLPLNE--TTLAEVLRQAGYAT---------------------GMIGKWhlgqreAYLPNSRG-FDYYFGIPFSHDSSLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 194 FKKNAVKEVPVHNNPAS--------VTIHPYHPDTELFRYTYAT-----FYDRIQDSDTALGELIEMLKTDGELDNTFVF 260
Cdd:cd16161 136 DRYAQFATDFIQRASAKdrpfflyaALAHVHVPLANLPRFQSPTsgrgpYGDALQEMDDLVGQIMDAVKHAGLKDNTLTW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 261 YFGDNG------------------GSLPGT--KGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLH 320
Cdd:cd16161 216 FTSDNGpwevkcelavgpgtgdwqGNLGGSvaKASTWEGGHREPAIVYWPGR------IPANSTSAALVSTLDIFPTVVA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 321 LAGITVPEG--IDGTpflgeDISLKQLNdrdevyGYGDRFDELYAFNRTVRKGRFKYSRNFQPYhskslyafyrykqaaf 398
Cdd:cd16161 290 LAGASLPPGriYDGK-----DLSPVLFG------GSKTGHRCLFHPNSGAAGAGALSAVRCGDY---------------- 342
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1782095189 399 rewKELYAKGMLNEIQKRFFEPQGAEE--LYDLSVDPYETKNL 439
Cdd:cd16161 343 ---KAHYATGGALACCGSTGPKLYHDPplLFDLEVDPAESFPL 382
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
44-323 |
2.34e-22 |
|
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: 97.37 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGKEgvATPNVEKLAAEGIVFNNAYCNAPVSSAARS--TLITGCYAPRLGVSFhRKLQKM 121
Cdd:cd16015 1 PNVIVILLESFSDPYIDKDVGGED--LTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGS-YTLYKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 122 PMPEGLnmfPSYLRKAGYHTS---NATKTDYNC-----------FLDKTAWDVVEGKIGEW--------RN-----RPDK 174
Cdd:cd16015 78 NPLPSL---PSILKEQGYETIfihGGDASFYNRdsvypnlgfdeFYDLEDFPDDEKETNGWgvsdeslfDQaleelEELK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 175 RKPFFHVYTNAVTHEGKLQFKKNAVKEVPVHNNPASVTihpyhpdtelfrytyaTFYDRIQDSDTALGELIEMLKTDGEL 254
Cdd:cd16015 155 KKPFFIFLVTMSNHGPYDLPEEKKDEPLKVEEDKTELE----------------NYLNAIHYTDKALGEFIEKLKKSGLY 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782095189 255 DNT-FVFYfGDNGGSLPGTKGYTTEGGL---QVPLVVYVPRKwreflpvKVGQRVDGFVSFMDLGPTLLHLAG 323
Cdd:cd16015 219 ENTiIVIY-GDHLPSLGSDYDETDEDPLdlyRTPLLIYSPGL-------KKPKKIDRVGSQIDIAPTLLDLLG 283
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
44-436 |
1.74e-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: 293773 [Multi-domain] Cd Length: 372 Bit Score: 90.49 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGKEGVATPNVEKLAAEGIVFNNAYCNaPVSSAARSTLITGCYAPRLGVSF--------- 114
Cdd:cd16154 1 PNILLIIADDQGLDSSAQYSLSSDLPVTPTLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAvpdelllse 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 115 ---HRKLQKMPMPEGLNMfpSYLRKagYHTSNATKTDYNCFL-------------DKTAWDVVEGKIGE----------- 167
Cdd:cd16154 80 etlLQLLIKDATTAGYSS--AVIGK--WHLGGNDNSPNNPGGipyyagilgggvqDYYNWNLTNNGQTTnsteyattklt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 168 -----WRNrpDKRKPFFhvytnavthegkLQFKKNAvKEVPVHNNPA---SVTIHPYHPDTELFRYTYatFYDRIQDSDT 239
Cdd:cd16154 156 nlaidWID--QQTKPWF------------LWLAYNA-PHTPFHLPPAelhSRSLLGDSADIEANPRPY--YLAAIEAMDT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 240 ALGELIEMLkTDGELDNTFVFYFGDNG---------GSLPGTKGYTTEGGLQVPLVVY---VPRkwreflpvkVGQRVDG 307
Cdd:cd16154 219 EIGRLLASI-DEEERENTIIIFIGDNGtpgqvvdlpYTRNHAKGSLYEGGINVPLIVSgagVER---------ANERESA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 308 FVSFMDLGPTLLHLAGITVPEGIDGTPFL----GEDISLKQlndrdevYGYGDRFDELYAFNRTVRKgrfkysrnfqpyh 383
Cdd:cd16154 289 LVNATDLYATIAELAGVDAAEIHDSVSFKpllsDVNASTRQ-------YNYTEYESPTTTGWATRNQ------------- 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1782095189 384 skslyafyRYKqaafrewkelyakgmlneiqKRFFEpQGAEELYDLSVDPYET 436
Cdd:cd16154 349 --------YYK--------------------LIESE-NGQEELYDLINDPSEQ 372
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
44-322 |
4.27e-19 |
|
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: 86.71 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYNDGKEgvATPNVEKLAAEGIVFNNAYCNAPVSSAA-RSTLITGCYAPRLGVSFHrklqKMP 122
Cdd:cd00016 1 KHVVLIVLDGLGADDLGKAGNPAP--TTPNLKRLASEGATFNFRSVSPPTSSAPnHAALLTGAYPTLHGYTGN----GSA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 123 MPEGLNM----------FPSYLRKAGYhtsnatktdyncfldktAWDVVEG-KIGEWRNrpdKRKPFF-HVYTNAVTHEG 190
Cdd:cd00016 75 DPELPSRaagkdedgptIPELLKQAGY-----------------RTGVIGLlKAIDETS---KEKPFVlFLHFDGPDGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 191 klqfkknavkevpvhnnpasvtiHPYHPDTElfrytyaTFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSL- 269
Cdd:cd00016 135 -----------------------HAYGPNTP-------EYYDAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGGIDk 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 270 -------PGTKGYTTEGGLQVPLVVYVPRKWReflpvkvGQRVDGFVSFMDLGPTLLHLA 322
Cdd:cd00016 185 ghggdpkADGKADKSHTGMRVPFIAYGPGVKK-------GGVKHELISQYDIAPTLADLL 237
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
44-455 |
6.35e-19 |
|
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: 90.20 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGV--SFHRKLQKM 121
Cdd:cd16158 2 PNIVLLFADDLGYGDLGCY--GHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVypGVFYPGSRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 122 PMPEGLNMFPSYLRKAGYHTSNATKtdyncfldktaWDVVEGKIGEWRnrpDKRKPFFHVYTNAVTH-EGKLQ------- 193
Cdd:cd16158 80 GLPLNETTIAEVLKTVGYQTAMVGK-----------WHLGVGLNGTYL---PTHQGFDHYLGIPYSHdQGPCQnltcfpp 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 194 -----------------FKKNAVKEVPV--------HNNPASVTI-----------------HPYHPDTELFRYTYAT-- 229
Cdd:cd16158 146 nipcfggcdqgevpcplFYNESIVQQPVdlltleerYAKFAKDFIadnakegkpfflyyashHTHYPQFAGQKFAGRSsr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 230 --FYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNG------------GSLPGTKGYTTEGGLQVPLVVYVPRKwre 295
Cdd:cd16158 226 gpFGDALAELDGSVGELLQTLKENGIDNNTLVFFTSDNGpstmrksrggnaGLLKCGKGTTYEGGVREPAIAYWPGR--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 296 flpVKVGqRVDGFVSFMDLGPTLLHLAGITVPE----GIDGTPFL-GEDISLKQL-----NDRDEVYGygdrfdeLYAfn 365
Cdd:cd16158 303 ---IKPG-VTHELASTLDILPTIAKLAGAPLPNvtldGVDMSPILfEQGKSPRQTffyypTSPDPDKG-------VFA-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 366 rtVRKGRFKysrnfqpyhskslyAFYrYKQAAFREwkelyakGMLNEIQKRFFEPQGAEE---LYDLSVDPYETKNLATV 442
Cdd:cd16158 370 --VRWGKYK--------------AHF-YTQGAAHS-------GTTPDKDCHPSAELTSHDpplLFDLSQDPSENYNLLGL 425
|
490
....*....|...
gi 1782095189 443 PVYRSTLENLRIL 455
Cdd:cd16158 426 PEYNQVLKQIQQV 438
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
43-374 |
1.43e-18 |
|
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: 89.06 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLY-NDGKEgvaTPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLG---VSFHRKL 118
Cdd:cd16157 1 KPNIILMLMDDMGWGDLGVFgEPSRE---TPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGfytTNAHARN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 119 QKMP------MPEGLNMFPSYLRKAGYHTSNATK------TDY--------------NC----FLDKTA--------WDV 160
Cdd:cd16157 78 AYTPqnivggIPDSEILLPELLKKAGYRNKIVGKwhlghrPQYhplkhgfdewfgapNChfgpYDNKAYpnipvyrdWEM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 161 V---------EGKIGE--------------WRNRPDKRKPFFHVYTNAVTHEgklqfkknavkevPVHNNPasvtihPYH 217
Cdd:cd16157 158 IgryyeefkiDKKTGEsnltqiylqealefIEKQHDAQKPFFLYWAPDATHA-------------PVYASK------PFL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 218 PDTELFRYTyatfyDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLPGTKGY-------------TTEGGLQVP 284
Cdd:cd16157 219 GTSQRGLYG-----DAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAALISAPEQggsngpflcgkqtTFEGGMREP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 285 LVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEG--IDGTPFLGEdISLKQLNDRDEVYgYgdRFDELY 362
Cdd:cd16157 294 AIAWWPGH------IKPGQVSHQLGSLMDLFTTSLALAGLPIPSDraIDGIDLLPV-LLNGKEKDRPIFY-Y--RGDELM 363
|
410
....*....|..
gi 1782095189 363 AfnrtVRKGRFK 374
Cdd:cd16157 364 A----VRLGQYK 371
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
65-336 |
2.37e-18 |
|
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293781 [Multi-domain] Cd Length: 366 Bit Score: 87.21 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 65 GKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYaPRLGVSFHRKlqkmpmpEGLNmfPSY------LRKAG 138
Cdd:cd16171 20 GNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLF-THLTESWNNY-------KGLD--PNYptwmdrLEKHG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 139 YHTSNATKTDYncfldKTAWDVVEGKIGEW-RNRP----DKRKPFFHVYTNAVTHEGKLQFKKN---AV----KEVPVHN 206
Cdd:cd16171 90 YHTQKYGKLDY-----TSGHHSVSNRVEAWtRDVPfllrQEGRPTVNLVGDRSTVRVMLKDWQNtdkAVhwirKEAPNLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 207 NPASVTI-----HPYHPDT--ELF---RYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGG-SLPGTKGY 275
Cdd:cd16171 165 QPFALYLglnlpHPYPSPSmgENFgsiRNIRAFYYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGElAMEHRQFY 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782095189 276 TT---EGGLQVPLVVYVPRkwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFL 336
Cdd:cd16171 245 KMsmyEGSSHVPLLIMGPG-------IKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLL 301
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
43-391 |
9.74e-18 |
|
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: 86.33 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISKHYLSLYndgkeGVATPN---VEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSFHRKLQ 119
Cdd:cd16160 1 KPNIVLFFADDMGYGDLASY-----GHPTQErgpIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 120 kmpMPEGLNMFPSY-------LRKAGYHTS---------NATKTDYNCFLDKT-AWDVVeGKI------------GEWRN 170
Cdd:cd16160 76 ---LPWDIGGLPKTevtmaeaLKEAGYTTGmvgkwhlgiNENNHSDGAHLPSHhGFDFV-GTNlpftnswacddtGRHVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 171 RPDKRKPFfhVYTNAVTHEGKLQFKKNAVKEVpvhnNPASVTIH-----PY-------HPDTELF----------RYTYA 228
Cdd:cd16160 152 FPDRSACF--LYYNDTIVEQPIQHEHLTETLV----GDAKSFIEdnqenPFflyfsfpQTHTPLFaskrfkgkskRGRYG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 229 tfyDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNG------------GSLPGTKGYTTEGGLQVPLVVYvprkWREF 296
Cdd:cd16160 226 ---DNINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGphveycleggstGGLKGGKGNSWEGGIRVPFIAY----WPGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 297 LPVKVGQRVdgfVSFMDLGPTLLHLAGITVPE-----GIDGTPFLGEDISlkqlNDRDEV-YGYGDRfdeLYAfnrtVRK 370
Cdd:cd16160 299 IKPRVSHEV---VSTMDIFPTFVDLAGGTLPTdriydGLSITDLLLGEAD----SPHDDIlYYCCSR---LMA----VRY 364
|
410 420
....*....|....*....|.
gi 1782095189 371 GRFKYSRNFQPYHSKSLYAFY 391
Cdd:cd16160 365 GSYKIHFKTQPLPSQESLDPN 385
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
44-472 |
1.34e-15 |
|
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: 79.73 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 44 PNFVWFMAEDISKHYLSLYndGKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLGVSfhrkLQKMPM 123
Cdd:cd16156 1 KQFIFIMTDTQRWDMVGCY--GNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSW----TNCMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 124 PEGLNMFPSYLRKAGYHTSNATK-----TDY------------------NCFLD------KTAW----DVVEGK-IGE-- 167
Cdd:cd16156 75 GDNVKTIGQRLSDNGIHTAYIGKwhldgGDYfgngicpqgwdpdywydmRNYLDelteeeRRKSrrglTSLEAEgIKEef 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 168 -WRNRPDKR----------KPFFHVYTNAVTHEGKLQFKKNAVK----EVP----VHNNPASVTIH-------PYHPDTE 221
Cdd:cd16156 155 tYGHRCTNRaldfiekhkdEDFFLVVSYDEPHHPFLCPKPYASMykdfEFPkgenAYDDLENKPLHqrlwagaKPHEDGD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 222 LFRYTYATFYDRIQDSDTALGELIEmlKTDGELDNTFVFYFGDNGGSLpGTKGYTTEGGL------QVPLVVYVPRKwre 295
Cdd:cd16156 235 KGTIKHPLYFGCNSFVDYEIGRVLD--AADEIAEDAWVIYTSDHGDML-GAHKLWAKGPAvydeitNIPLIIRGKGG--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 296 flpVKVGQRVDGFVSFMDLGPTLLHLAGITVPEGIDGTPFLgEDISLKQLNDRDEVYGYGDRF----DELYAFN--RTVR 369
Cdd:cd16156 309 ---EKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESIL-ATIEDPEIPENRGVFVEFGRYevdhDGFGGFQpvRCVV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 370 KGRFKYSRNFqpyhskslyafyrykqaafrewkelyakgmlneiqkrffepQGAEELYDLSVDPYETKNLATVPVYRSTL 449
Cdd:cd16156 385 DGRYKLVINL-----------------------------------------LSTDELYDLEKDPYEMHNLIDDPDYADVR 423
|
490 500
....*....|....*....|....*
gi 1782095189 450 ENLRILLKGKLLEENDL--GFYPEC 472
Cdd:cd16156 424 DQLHDELLDYMNETRDPfrGYYWEC 448
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
42-325 |
1.78e-10 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 62.26 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 42 ERPNFVWFMAEDISKHYLSLYNDGKEgvATPNVEKLAAEGIVFNNAYCNAPVSSAA-RSTLitgcyaprlgvSFHRKLQK 120
Cdd:cd16017 1 KPKNVVLVIGESARRDHMSLYGYPRD--TTPFLSKLKKNLIVFDNVISCGTSTAVSlPCML-----------SFANRENY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 121 MPMPEGLNmFPSYLRKAGYHT---SN-ATKTDYNCFLDKTAWDVvegkigewrnrpdKRKPFFHVYTNAVTHEGKL--QF 194
Cdd:cd16017 68 DRAYYQEN-LIDLAKKAGYKTywiSNqGGCGGYDTRISAIAKIE-------------TVFTNKGSCNSSNCYDEALlpLL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 195 KKNavkeVPVHNNPASVTIH------PYH---PDTelFRYTYATFYDRIQDS----------------DTALGELIEMLK 249
Cdd:cd16017 134 DEA----LADSSKKKLIVLHlmgshgPYYdryPEE--FAKFTPDCDNELQSCskeelinaydnsilytDYVLSQIIERLK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 250 TDGEldNTFVFYF-------GDNGGSLPGTkGYTTEGGLQVPLVVYVPRKWREFLPV-KVGQRVDGFVSFMDLGPTLLHL 321
Cdd:cd16017 208 KKDK--DAALIYFsdhgeslGENGLYLHGA-PYAPKEQYHVPFIIWSSDSYKQRYPVeRLRANKDRPFSHDNLFHTLLGL 284
|
....
gi 1782095189 322 AGIT 325
Cdd:cd16017 285 LGIK 288
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
43-332 |
2.31e-10 |
|
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: 63.46 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 43 RPNFVWFMAEDISkhylslYND----GKEGVATPNVEKLAAEGIVFNNAYCNAPVSSAARSTLITGCYAPRLG-VSFHRK 117
Cdd:cd16159 1 KPNIVLFMADDLG------IGDvgcfGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGmASSHGM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 118 LQKM------PMPEGLNMFPSYLRKAGYHT----------SNATKTDYNCFLDKTAWDVV--------------EGKIGE 167
Cdd:cd16159 75 RVILftassgGLPPNETTFAEVLKQQGYSTaligkwhlglHCESRNDFCHHPLNHGFDYFyglpltnlkdcgdgSNGEYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 168 WRNRPDK------------------------RKPFFHV-------------------YTNAVTHEG-------------K 191
Cdd:cd16159 155 LSFDPLFplltafvlitaltiflllylgavsKRFFVFLlilsllfislfflllitnrYFNCILMRNhevveqpmslenlT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 192 LQFKKNAVKEVPVHNNPASVTIHPY-HPDTELF-------RYTYATFYDRIQDSDTALGELIEMLKTDGELDNTFVFYFG 263
Cdd:cd16159 235 QRLTKEAISFLERNKERPFLLVMSFlHVHTALFtskkfkgRSKHGRYGDNVEEMDWSVGQILDALDELGLKDNTFVYFTS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 264 DNGGSLP-----------------GTKGYTTEGGLQVPLVVYVPRKwreflpVKVGQRVDGFVSFMDLGPTLLHLAGITV 326
Cdd:cd16159 315 DNGGHLEeisvggeygggnggiygGKKMGGWEGGIRVPTIVRWPGV------IPPGSVIDEPTSLMDIFPTVAALAGAPL 388
|
....*...
gi 1782095189 327 PEG--IDG 332
Cdd:cd16159 389 PSDriIDG 396
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
67-323 |
4.39e-08 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 54.90 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 67 EGVATPNVEKLAAEGIVFNNAYCNAP-VSSAARSTLITGCYAPRLGVS----FHRKLQKMPMPEGLNMFPSYLR------ 135
Cdd:cd16018 18 RAGLTPNLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYPESHGIVgnyfYDPKTNEEFSDSDWVWDPWWIGgepiwv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 136 ---KAGYHTsnatktdYNCFldktaWDVVEGKIGEWRNRPDKRKPFFHVYTNAVTHEgklqFKKNAVKEVPVHNNPASVT 212
Cdd:cd16018 98 taeKAGLKT-------ASYF-----WPGSEVAIIGYNPTPIPLGGYWQPYNDSFPFE----ERVDTILEWLDLERPDLIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782095189 213 IHPYHPDTELFRYTYAT--FYDRIQDSDTALGELIEMLKTDGELDNTFVFYFGDNGGSLPGTKGY-TTEGGLQVPLVVYV 289
Cdd:cd16018 162 LYFEEPDSAGHKYGPDSpeVNEALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDVGTHGYdNELPDMRAIFIARG 241
|
250 260 270
....*....|....*....|....*....|....
gi 1782095189 290 PRkwreflpVKVGQRVDGFvSFMDLGPTLLHLAG 323
Cdd:cd16018 242 PA-------FKKGKKLGPF-RNVDIYPLMCNLLG 267
|
|
| HEAT |
COG1413 |
HEAT repeat [General function prediction only]; |
508-583 |
2.02e-05 |
|
HEAT repeat [General function prediction only];
Pssm-ID: 441023 [Multi-domain] Cd Length: 137 Bit Score: 44.62 E-value: 2.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782095189 508 KDAKPAISKALNSSDPVERYWGATVCASFGGEAVslYKELELLTVDTQAFVRSRAIVALSRMGKVNPVPLMKEALQ 583
Cdd:COG1413 15 PAAVPALIAALADEDPDVRAAAARALGRLGDPRA--VPALLEALKDPDPEVRAAAAEALGRIGDPEAVPALIAALK 88
|
|
| HEAT |
COG1413 |
HEAT repeat [General function prediction only]; |
508-583 |
6.28e-05 |
|
HEAT repeat [General function prediction only];
Pssm-ID: 441023 [Multi-domain] Cd Length: 137 Bit Score: 43.08 E-value: 6.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782095189 508 KDAKPAISKALNSSDPVERYWGATVCASFGGEAVslYKELELLTVDTQAFVRSRAIVALSRMGKVNPVPLMKEALQ 583
Cdd:COG1413 46 PRAVPALLEALKDPDPEVRAAAAEALGRIGDPEA--VPALIAALKDEDPEVRRAAAEALGRLGDPAAVPALLEALK 119
|
|
| |
