|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
24-472 |
1.57e-153 |
|
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: 442.33 E-value: 1.57e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 104 VRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 183 CGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGV 262
Cdd:cd16027 156 PYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 263 LNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSYaifgsktih 342
Cdd:cd16027 215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFIDLAPTLLDLAGIEPPEY--------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 343 LTGRSLLPALEAE--PLWATVFGSQSHHEVTmSYPMRSVQHRHFRLVHNLNFkmpfpidqdfyvsptfqdllnrttagqp 420
Cdd:cd16027 285 LQGRSFLPLLKGEkdPGRDYVFAERDRHDET-YDPIRSVRTGRYKYIRNYMP---------------------------- 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 4506919 421 tgwykdlrhyyyrarWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQ 472
Cdd:cd16027 336 ---------------EELYDLKNDPDELNNLADDPEYAEVLEELRAALDAWM 372
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
21-478 |
2.03e-82 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 260.97 E-value: 2.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFN 99
Cdd:COG3119 23 RP-NILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKVrSLPLLLSQAGVRTGIIGKKHvgpetVYpFDFAYTEEngsvlqvgrnitrikllVRKFLQTQ--DDRPFFLYVAF 177
Cdd:COG3119 102 PPDEP-TLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AIDFLERQadKDKPFFLYLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 178 HDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYDPLDVLVP-YFVP---NTPAARADLAAQYTTVGRMDQGVGLV 253
Cdd:COG3119 158 NAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPrdlTEEELRRARAAYAAMIEEVDDQVGRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 254 LQELRDAGVLNDTLVIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSI 328
Cdd:COG3119 217 LDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GSVSDALVSLIDLLPTLLDLAGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 329 PYPSyaifgsktiHLTGRSLLPALE-AEPLWATVFgsqsHHEVTMSYPMRSVQHRHFRLVHNlnfkmpfpidqdfyvspt 407
Cdd:COG3119 296 PIPE---------DLDGRSLLPLLTgEKAEWRDYL----YWEYPRGGGNRAIRTGRWKLIRY------------------ 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506919 408 fqdllnrttagqptgwykdlrhYYYRARWELYDRSRDPHETQNLATDprFAQLLEMLRDQLAKWQWETHDP 478
Cdd:COG3119 345 ----------------------YDDDGPWELYDLKNDPGETNNLAAD--YPEVVAELRALLEAWLKELGDP 391
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
21-468 |
2.95e-66 |
|
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: 219.71 E-value: 2.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVhhFN 99
Cdd:cd16031 1 KRPNIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPL--FD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKvrSLPLLLSQAGVRTGIIGKKHVGPETVYP---FDF------------AYTEENGSVLQVGRNITRIKL-LVRKFL 163
Cdd:cd16031 79 ASQP--TYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydPEFIENGKRVGQKGYVTDIITdKALDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 164 QTQD-DRPFFLYVAFHDPHRCGHSQPQYGtfcEKFGNGEsgMGRIPDWTPQAYDPLdvlvPYFVPNTPAARADLA----- 237
Cdd:cd16031 157 KERDkDKPFCLSLSFKAPHRPFTPAPRHR---GLYEDVT--IPEPETFDDDDYAGR----PEWAREQRNRIRGVLdgrfd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 238 ----------AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG-------RTnLYWPGTAEPLLVSSPE 300
Cdd:cd16031 228 tpekyqrymkDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--FFLGehglfdkRL-MYEESIRVPLIIRDPR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 301 HPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPALEAEPL--WAT-----VFGSQSHHEVTMS 373
Cdd:cd16031 305 LIKA-GTVVDALVLNIDFAPTILDLAGVPIPE---------DMQGRSLLPLLEGEKPvdWRKefyyeYYEEPNFHNVPTH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 374 YPMRsvqhrhfrlvhnlnfkmpfpidqdfyvsptfqdllnrttagqpTGWYKDLRHYYYRARWELYDRSRDPHETQNLAT 453
Cdd:cd16031 375 EGVR-------------------------------------------TERYKYIYYYGVWDEEELYDLKKDPLELNNLAN 411
|
490
....*....|....*
gi 4506919 454 DPRFAQLLEMLRDQL 468
Cdd:cd16031 412 DPEYAEVLKELRKRL 426
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
24-347 |
3.23e-62 |
|
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: 203.05 E-value: 3.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNsfD 102
Cdd:cd16022 2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRSLPLLLSQAGVRTGIIGKKHvgpetvypfDFAyteengsvlqvgrnitrikllvRKFLQTQD-DRPFFLYVAFHDPH 181
Cdd:cd16022 80 DEPTLAELLKEAGYRTALIGKWH---------DEA----------------------IDFIERRDkDKPFFLYVSFNAPH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 182 rcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQELRDAG 261
Cdd:cd16022 129 -----------------------------PPFAY------------------------YAMVSAIDDQIGRILDALEELG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 262 VLNDTLVIFTSDNGIPFPSGR-----TNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaif 336
Cdd:cd16022 156 LLDNTLIVFTSDHGDMLGDHGlrgkkGSLYEGGIRVPFIVRWPGKIPA-GQVSDALVSLLDLLPTLLDLAGIEPPE---- 230
|
330
....*....|.
gi 4506919 337 gsktiHLTGRS 347
Cdd:cd16022 231 -----GLDGRS 236
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
21-451 |
1.58e-60 |
|
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: 203.83 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGF-ESGAYNnSAIATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTGLPQHQNG---MYGLHQDVH 96
Cdd:cd16025 2 RP-NILLILADDLGFsDLGCFG-GEIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGmgtMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 97 HFNSF--DKVRSLPLLLSQAGVRTGIIGKKHVGPETVYpFDFAYTEengsvlqvgrnitriKLLvrKFLQTQ--DDRPFF 172
Cdd:cd16025 79 GYEGYlpDSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------------KAI--EYIDEQkaPDKPFF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 173 LYVAF---HDPHrcgHSQPQY-----GTFcekfgngESG--------------MGRIPDWTPQAYDPLDvlvpyfVPN-- 228
Cdd:cd16025 141 LYLAFgapHAPL---QAPKEWidkykGKY-------DAGwdalreerlerqkeLGLIPADTKLTPRPPG------VPAwd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 229 --TPAARADL-------AAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYW 287
Cdd:cd16025 205 slSPEEKKLEarrmevyAAM---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 288 PGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTPTILDWFSIPYPSyAIFGSKTIHLTGRSLLPALEAEPLWAT------- 360
Cdd:cd16025 282 GGIRTPLIVSWPKGIKAKGGIRHQFAHVIDIAPTILELAGVEYPK-TVNGVPQLPLDGVSLLPTLDGAAAPSRrrtqyfe 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 361 VFGSqshhevtmsypmRSVQHRHFRLVHNlnfkmpfpidqdfyvsptfqdllnrttaGQPTGWYkdlrhyyyrARWELYD 440
Cdd:cd16025 361 LFGN------------RAIRKGGWKAVAL----------------------------HPPPGWG---------DQWELYD 391
|
490
....*....|.
gi 4506919 441 RSRDPHETQNL 451
Cdd:cd16025 392 LAKDPSETHDL 402
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-468 |
1.61e-56 |
|
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: 192.39 E-value: 1.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAF----TSVSSCSPSRASLLTGlpqhqngMYGLH-QD 94
Cdd:cd16155 2 KP-NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMTG-------RTLFHaPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 95 VHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVgpetvypfDFAyteeNGSVlqvgrnitrikllvrKFLQ--TQDDRPFF 172
Cdd:cd16155 74 GGKAAIPSDDKTWPETFKKAGYRTFATGKWHN--------GFA----DAAI---------------EFLEeyKDGDKPFF 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 173 LYVAFHDPHrcghsQPQYGT--FCEKFGNGEsgmgrIPDwtPQAYDPL------------DVLVPYfvPNTPAA-RADLA 237
Cdd:cd16155 127 MYVAFTAPH-----DPRQAPpeYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 238 AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYV 313
Cdd:cd16155 193 EYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGPGIPK--GKRRDALV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 314 SLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPALEAEplwatvfgSQSHHEvTMSYPMRSVQhrhfRLVHNLNFK 393
Cdd:cd16155 271 YLQDVFPTLCELAGIEIPE---------SVEGKSLLPVIRGE--------KKAVRD-TLYGAYRDGQ----RAIRDDRWK 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506919 394 MpfpidqDFYVsptfqdllnrttagqptgwyKDLRHYyyrarwELYDRSRDPHETQNLATDPRFAQLLEMLRDQL 468
Cdd:cd16155 329 L------IIYV--------------------PGVKRT------QLFDLKKDPDELNNLADEPEYQERLKKLLAEL 371
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-328 |
4.28e-54 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 183.78 E-value: 4.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 23 RNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884 1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 102 DKVRSLPLLLSQAGVRTGIIGKKHVGP-----ETVYPFDFAYTEENGSVLQVGRNITRI---------KLLVRKFLQ--T 165
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 166 QDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYdpldvlvPYFVPNTPAARADLAAQYTTVGR 245
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPPYYPDRY---------------------PEKY-------ATFKPSSCSEEQLLNSYDNTLLY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 246 MDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLD 317
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVSHVD 287
|
330
....*....|.
gi 4506919 318 LTPTILDWFSI 328
Cdd:pfam00884 288 LFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-477 |
8.90e-52 |
|
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: 180.88 E-value: 8.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNSF- 101
Cdd:cd16033 2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL---NNVENAGAYs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 102 ----DKVRSLPLLLSQAGVRTGIIGKKHVGPETVyPFDFAYtEENGSVLQ------VGRNITRIkllvRKFLqtQDDRPF 171
Cdd:cd16033 79 rglpPGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEML----EELA--ADDKPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 172 FLYVAFHDPHrcghsQPqYgtfcekfgngesgmgRIPDWTPQAYDPLDVLVP--YFVP--NTPAA--------------- 232
Cdd:cd16033 151 FLRVNFWGPH-----DP-Y---------------IPPEPYLDMYDPEDIPLPesFADDfeDKPYIyrrerkrwgvdtede 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 233 ---RADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAE-----PLLVSSPEHpKR 304
Cdd:cd16033 210 edwKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEetyriPLIIKWPGV-IA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 305 WGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPAL--EAEPLWATVFGSQSH-HEVTmsYPMRSVQH 381
Cdd:cd16033 289 AGQVVDEFVSLLDLAPTILDLAGVDVPP---------KVDGRSLLPLLrgEQPEDWRDEVVTEYNgHEFY--LPQRMVRT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 382 RHFRLVHNlnfkmPFPIDqdfyvsptfqdllnrttagqptgwykdlrhyyyrarwELYDRSRDPHETQNLATDPRFAQLL 461
Cdd:cd16033 358 DRYKYVFN-----GFDID-------------------------------------ELYDLESDPYELNNLIDDPEYEEIL 395
|
490
....*....|....*.
gi 4506919 462 EMLRDQLAKWQWETHD 477
Cdd:cd16033 396 REMRTRLYEWMEETGD 411
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-471 |
1.11e-48 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293763 [Multi-domain] Cd Length: 421 Bit Score: 173.11 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGL--PQHQNGMYGLHQDVHHFNS 100
Cdd:cd16144 2 NIVLILVDDlGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQypARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 101 F-----------DKVRSLPLLLSQAGVRTGIIGKKHVGPE-TVYP----FD---------------FAYTEENGSVLQVG 149
Cdd:cd16144 82 KlipppsttrlpLEEVTIAEALKDAGYATAHFGKWHLGGEgGYGPedqgFDvniggtgnggppsyyFPPGKPNPDLEDGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 150 RNITRIKLLVR---KFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAydpldvlvpyfv 226
Cdd:cd16144 162 EGEYLTDRLTDeaiDFIEQNKDKPFFLYLSHYAVH-----------------------------TPIQ------------ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 227 pntpaARADLAAQYTTVGR-----------------MDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IP 277
Cdd:cd16144 201 -----ARPELIEKYEKKKKglrkgqknpvyaamiesLDESVGRILDALEELGLADNTLVIFTSDNGglstrggpptsnAP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSYAifgsktiHLTGRSLLPALEAEpl 357
Cdd:cd16144 276 LRGGKGSLYEGGIRVPLIVRWPGVIKP-GSVSDVPVIGTDLYPTFLELAGGPLPPPQ-------HLDGVSLVPLLKGG-- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 358 watvfgsqshhevTMSYPMRS-VQHrhfrlvhnlnfkmpFPIDQDFYVSPtfqdllnrTTA---GQptgwYKdLRHYYYR 433
Cdd:cd16144 346 -------------EADLPRRAlFWH--------------FPHYHGQGGRP--------ASAirkGD----WK-LIEFYED 385
|
490 500 510
....*....|....*....|....*....|....*...
gi 4506919 434 ARWELYDRSRDPHETQNLATDprFAQLLEMLRDQLAKW 471
Cdd:cd16144 386 GRVELYNLKNDIGETNNLAAE--MPEKAAELKKKLDAW 421
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-392 |
7.76e-46 |
|
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: 162.71 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 23 RNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNS- 100
Cdd:cd16037 1 PNILIIMSDEhNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD--------NAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 101 --FDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFdFAYTeengsvlqvgRNITRiklLVRKFLQTQ--DDRPFFLYVA 176
Cdd:cd16037 73 pyDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVTE---AAVDWLREEaaDDKPWFLFVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 177 FHDPHrcghsqpqygtFcekfgngesgmgriPDWTPQA-YDpldvlvpYFVpntpaaRADLAAQYTTVGRMDQGVGLVLQ 255
Cdd:cd16037 139 FVAPH-----------F--------------PLIAPQEfYD-------LYV------RRARAAYYGLVEFLDENIGRVLD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 256 ELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSIPYP 331
Cdd:cd16037 181 ALEELGLLDNTLIIYTSDHGDMLGErglwGKSTMYEESVRVPMIISGPGIPA--GKRVKTPVSLVDLAPTILEAAGAPPP 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4506919 332 SyaifgsktiHLTGRSLLPALEAEPLWA-TVFgSQSH-HEVTMsyPMRSVQHRHFRLVHNLNF 392
Cdd:cd16037 259 P---------DLDGRSLLPLAEGPDDPDrVVF-SEYHaHGSPS--GAFMLRKGRWKYIYYVGY 309
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-477 |
1.31e-45 |
|
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: 164.72 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGmyglHQDVHHFNSFDKvrslPLLLS---QA 114
Cdd:cd16150 17 GHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHLLRPDE----PNLLKtlkDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 115 GVRTGIIGKKHVGPETVYPFDFAYTEEngsvLQVGRNITRIKllvrkflQTQDDRPFFLYVAFHDPHrcghsqPQYGtfC 194
Cdd:cd16150 89 GYHVAWAGKNDDLPGEFAAEAYCDSDE----ACVRTAIDWLR-------NRRPDKPFCLYLPLIFPH------PPYG--V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 195 EKfgngesgmgriPDWTpqAYDPLDVLVPyfVPNTPAARADL-----------------------AAQYTTVGRMDQGVG 251
Cdd:cd16150 150 EE-----------PWFS--MIDREKLPPR--RPPGLRAKGKPsmlegiekqgldrwseerwrelrATYLGMVSRLDHQFG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 252 LVLQELRDAGVLNDTLVIFTSDNGipfpsGRTNLY-----WPGTAE------PLLVSSPEHPKrwGQVSEAYVSLLDLTP 320
Cdd:cd16150 215 RLLEALKETGLYDDTAVFFFSDHG-----DYTGDYglvekWPNTFEdcltrvPLIIKPPGGPA--GGVSDALVELVDIPP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 321 TILDWFSIPyPSYAIFgsktihltGRSLLPALEAEP--LWATVF-------GSQSHHEVTMS----YPMRSVQHRHFRLV 387
Cdd:cd16150 288 TLLDLAGIP-LSHTHF--------GRSLLPVLAGETeeHRDAVFseggrlhGEEQAMEGGHGpydlKWPRLLQQEEPPEH 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 388 ------HNLNFKmpfpidqdfYVsptfqdllnRTTAGQPtgwykdlrhyyyrarwELYDRSRDPHETQNLATDPRFAQLL 461
Cdd:cd16150 359 tkavmiRTRRYK---------YV---------YRLYEPD----------------ELYDLEADPLELHNLIGDPAYAEII 404
|
490
....*....|....*.
gi 4506919 462 EMLRDQLAKWQWETHD 477
Cdd:cd16150 405 AEMKQRLLRWMVETSD 420
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-471 |
1.80e-45 |
|
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: 163.87 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSfd 102
Cdd:cd16146 2 NVILILTDDQGYgDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWHTILGRERMRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRSLPLLLSQAGVRTGIIGKKHVGpeTVYP-------FDFAYTEENGSVLQVG-------------RNITRIK------ 156
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWHLG--DNYPyrpqdrgFDEVLGHGGGGIGQYPdywgndyfddtyyHNGKFVKtegyct 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 157 -LLVR---KFLQTQDDRPFFLYVAFHDPHRcghsqpqygtfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAA 232
Cdd:cd16146 157 dVFFDeaiDFIEENKDKPFFAYLATNAPHG----------------------------------------PLQVPDKYLD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 233 R-------ADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPSGRTNLYWP-------------GTAE 292
Cdd:cd16146 197 PykdmgldDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRFNagmrgkkgsvyegGHRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 293 PLLVSSPEHpKRWGQVSEAYVSLLDLTPTILDWFSIPYPsyaifgsKTIHLTGRSLLPALEAE--PLWATVFGSQSHHEV 370
Cdd:cd16146 274 PFFIRWPGK-ILAGKDVDTLTAHIDLLPTLLDLCGVKLP-------EGIKLDGRSLLPLLKGEsdPWPERTLFTHSGRWP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 371 TMSYPMR--SVQHRHFRLVHNLNFKmpfpidqdfyvsptfqdllnrttagqptgwykdlrhyyyrarWELYDRSRDPHET 448
Cdd:cd16146 346 PPPKKKRnaAVRTGRWRLVSPKGFQ------------------------------------------PELYDIENDPGEE 383
|
490 500
....*....|....*....|...
gi 4506919 449 QNLATDprFAQLLEMLRDQLAKW 471
Cdd:cd16146 384 NDVADE--HPEVVKRLKAAYEAW 404
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-454 |
1.05e-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: 293764 [Multi-domain] Cd Length: 415 Bit Score: 159.30 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16145 2 NIIFILADDlGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETV--YP----FDF---------------AYTEENG------SVLQVGRNITRI 155
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPtkqgFDYfygyldqvhahnyypEYLWRNGekvplpNNVIPPLDEGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 156 KLLVR-------------KFLQTQDDRPFFLYVAFHDPHrcGHSQpqygtfcekfgngesgmgrIPDWTPQAYDPLDvLV 222
Cdd:cd16145 162 AGGGGgtyshdlftdealDFIRENKDKPFFLYLAYTLPH--APLQ-------------------VPDDGPYKYKPKD-PG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 223 PYFVPNTPAARADLAAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-----------------PFPSGRTNL 285
Cdd:cd16145 220 IYAYLPWPQPEKAYAAM---VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPhseggsehdpdffdsngPLRGYKRSL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 286 YWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPALEAEPlwatvfgsq 365
Cdd:cd16145 297 YEGGIRVPFIARWPGKIPA-GSVSDHPSAFWDFMPTLADLAGAEPPE---------DIDGISLLPTLLGKP--------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 366 shhevtmsypmRSVQHRHfrLVHNLNFKMpfpidqdfyvsptFQDLLNRttagqptGWYKDLRHYYYRARWELYDRSRDP 445
Cdd:cd16145 358 -----------QQQQHDY--LYWEFYEGG-------------GAQAVRM-------GGWKAVRHGKKDGPFELYDLSTDP 404
|
....*....
gi 4506919 446 HETQNLATD 454
Cdd:cd16145 405 GETNNLAAQ 413
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-452 |
1.17e-43 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293750 [Multi-domain] Cd Length: 399 Bit Score: 158.88 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 22 PRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-LPQ---------HQNGMYG 90
Cdd:cd16026 1 KPNIVVILADDLGYGDlGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGrYPVrvglpgvvgPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 91 LHQDVHhfnsfdkvrSLPLLLSQAGVRTGIIGKKHVG--PETvYP----FDFAY---------------TEENGSVLQVG 149
Cdd:cd16026 81 LPPDEI---------TIAEVLKKAGYRTALVGKWHLGhqPEF-LPtrhgFDEYFgipysndmwpfplyrNDPPGPLPPLM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 150 RNITRI----------KLLVRK---FLQTQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFgNGESGMGRIPDwtpqayd 216
Cdd:cd16026 151 ENEEVIeqpadqssltQRYTDEavdFIERNKDQPFFLYLAHTMPH-----VPLFAS--EKF-KGRSGAGLYGD------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 217 pldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTN 284
Cdd:cd16026 216 -------------------------VVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleygghggsaGPLRGGKGT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 285 LYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSYAIfgsktihLTGRSLLPALEAeplwatvfGS 364
Cdd:cd16026 271 TWEGGVRVPFIAWWPGVIPA-GTVSDELASTMDLLPTLAALAGAPLPEDRV-------IDGKDISPLLLG--------GS 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 365 QSHHEVTMSYPMrsvqHRHFRLVHNLNFKMPFPidqDFYVSPTFQDLLNRTTAGQPtgwykdlrhyyyrarwELYDRSRD 444
Cdd:cd16026 335 KSPPHPFFYYYD----GGDLQAVRSGRWKLHLP---TTYRTGTDPGGLDPTKLEPP----------------LLYDLEED 391
|
....*...
gi 4506919 445 PHETQNLA 452
Cdd:cd16026 392 PGETYNVA 399
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
22-457 |
8.62e-41 |
|
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: 151.96 E-value: 8.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 22 PRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSF 101
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNS--YFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 102 DKVRSLPLLLSQAGVRTGIIGK---KHVGPE-------TVYPFDFAYTEENGSVLQVGRNITR----------------- 154
Cdd:cd16030 80 PDAVTLPQYFKENGYTTAGVGKifhPGIPDGdddpaswDEPPNPPGPEKYPPGKLCPGKKGGKgggggpaweaadvpdea 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 155 ----------IKLLVRKFlqtQDDRPFFLYVAFHDPHRcghsqP---------QYGTFCEKFGNGESGMG----RIPDWT 211
Cdd:cd16030 160 ypdgkvadeaIEQLRKLK---DSDKPFFLAVGFYKPHL-----PfvapkkyfdLYPLESIPLPNPFDPIDlpevAWNDLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 212 --PQAYDPLDVLVPYFVPNTPAARADLAAQ--YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG------ 281
Cdd:cd16030 232 dlPKYGDIPALNPGDPKGPLPDEQARELRQayYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG--WHLGehghwg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 282 -RTNlyWPGTAE-PLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPALE-AEPLW 358
Cdd:cd16030 310 kHTL--FEEATRvPLIIRAPGVTKP-GKVTDALVELVDIYPTLAELAGLPAPP---------CLEGKSLVPLLKnPSAKW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 359 ATVFGSQSHHEVTMSYPMRSVQHRhfrlvhnlnfkmpfpidqdfYVSptfqdllnrttagqptgwYKDLRHYYYRarwEL 438
Cdd:cd16030 378 KDAAFSQYPRPSIMGYSIRTERYR--------------------YTE------------------WVDFDKVGAE---EL 416
|
490
....*....|....*....
gi 4506919 439 YDRSRDPHETQNLATDPRF 457
Cdd:cd16030 417 YDHKNDPNEWKNLANDPEY 435
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-474 |
3.37e-38 |
|
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: 143.52 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY----GLHQDVhhfnsfdkvRSLPLLLSQ 113
Cdd:cd16152 18 GCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFrngiPLPADE---------KTLAHYFRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 114 AGVRTGIIGKKHVGpetVYPFDFayteengsvlqvgrnITRIKLlvrKFLQT-QDDRPFFLYVAFHDPHrcgHsQPQYGT 192
Cdd:cd16152 89 AGYETGYVGKWHLA---GYRVDA---------------LTDFAI---DYLDNrQKDKPFFLFLSYLEPH---H-QNDRDR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 193 F------CEKFGNGesgmgripdWTPQAYDPLdvlvpyfvPNTpaARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDT 266
Cdd:cd16152 144 YvapegsAERFANF---------WVPPDLAAL--------PGD--WAEELPDYLGCCERLDENVGRIRDALKELGLYDNT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 267 LVIFTSDNGIPFPSgRTNLYWPGTAE-----PLLVSSPehPKRWGQVSEAYVSLLDLTPTILDWFSIPYPSYAIfgskti 341
Cdd:cd16152 205 IIVFTSDHGCHFRT-RNAEYKRSCHEssirvPLVIYGP--GFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQ------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 342 hltGRSLLPALEAEPL-WAT-VFGSQSHHEVTmsypmRSVQHRHFRL-VHNLNFKMPFPIDQDFYVSptfqdllnrttag 418
Cdd:cd16152 276 ---GRSLLPLVDGKVEdWRNeVFIQISESQVG-----RAIRTDRWKYsVAAPDKDGWKDSGSDVYVE------------- 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4506919 419 qptgwykdlrhyyyrarWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWE 474
Cdd:cd16152 335 -----------------DYLYDLEADPYELVNLIGRPEYREVAAELRERLLARMAE 373
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-483 |
7.57e-37 |
|
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: 141.75 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNSF---DKVRSLPLLLSQA 114
Cdd:cd16156 17 GCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCMalgDNVKTIGQRLSDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 115 GVRTGIIGKKHV-------------GPETVYPFDFA-YTEE----------NGSVLQVGRNIT-------RIKLLVRKFL 163
Cdd:cd16156 89 GIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnYLDElteeerrksrRGLTSLEAEGIKeeftyghRCTNRALDFI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 164 QTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFgngesgmgRIPDwTPQAYDPLDvlvpyfvpNTPA-ARADLAAQYTT 242
Cdd:cd16156 169 EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDF--------EFPK-GENAYDDLE--------NKPLhQRLWAGAKPHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 243 VGR---------------MDQGVGLVLQELRDagVLNDTLVIFTSDNGIPFpsGRTNLYWPGTAE-------PLLVSSPE 300
Cdd:cd16156 232 DGDkgtikhplyfgcnsfVDYEIGRVLDAADE--IAEDAWVIYTSDHGDML--GAHKLWAKGPAVydeitniPLIIRGKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 301 HPKRWGQVSeAYVSLLDLTPTILDWFSIPYPSYaifgsktihLTGRSLLPALEAE--PLWATVFGSQSHHEVTMS----- 373
Cdd:cd16156 308 GEKAGTVTD-TPVSHIDLAPTILDYAGIPQPKV---------LEGESILATIEDPeiPENRGVFVEFGRYEVDHDgfggf 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 374 YPMRSVQHRHFRLVHNLnfkmpfpIDQDfyvsptfqdllnrttagqptgwykdlrhyyyrarwELYDRSRDPHETQNLAT 453
Cdd:cd16156 378 QPVRCVVDGRYKLVINL-------LSTD-----------------------------------ELYDLEKDPYEMHNLID 415
|
490 500 510
....*....|....*....|....*....|....*
gi 4506919 454 DPRFAQLLEMLRDQLAKWQWETHDP-----WVCAP 483
Cdd:cd16156 416 DPDYADVRDQLHDELLDYMNETRDPfrgyyWECRP 450
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
21-333 |
8.59e-37 |
|
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficient of N-acetylglucosamine-6-sulfatase results in disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease. SULF1 encodes an extracellular heparan sulfate endosulfatase, that removes 6-O-sulfate groups from heparan sulfate chains of heparan sulfate proteoglycans (HSPGs).
Pssm-ID: 293766 [Multi-domain] Cd Length: 396 Bit Score: 139.99 E-value: 8.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGFESGAYNnsaiATPHLDA-LARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhFN 99
Cdd:cd16147 1 RP-NIVLILTDDQDVELGSMD----PMPKTKKlLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP---GG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKV-------RSLPLLLSQAGVRTGIIGK------KHVGPETVYP-FDFAYTEENGSV-----LQVGRNITRIK---- 156
Cdd:cd16147 73 GYPKFwqnglerSTLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDEWDGLVGNSTyynytLSNGGNGKHGVsypg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 157 -----LLVRK---FLQT--QDDRPFFLYVAFHDPHRCGHSQPQYGtfcekfgNGESGMGRIPDWTPQAYDPLDVlvPYFV 226
Cdd:cd16147 153 dyltdVIANKaldFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYA-------NLFPNVTAPPRPPPNNPDVSDK--PHWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 227 PNTPAARADLAAQYTTVGR--------MDQGVGLVLQELRDAGVLNDTLVIFTSDNGipF-------PSGRTNLYWPGTA 291
Cdd:cd16147 224 RRLPPLNPTQIAYIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG--YhlgqhrlPPGKRTPYEEDIR 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 4506919 292 EPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSIPYPSY 333
Cdd:cd16147 302 VPLLVRGPGIPA--GVTVDQLVSNIDLAPTILDLAGAPPPSD 341
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-388 |
1.13e-36 |
|
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: 138.10 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV--- 95
Cdd:cd16032 2 NILLIMADQlTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDnaaeFPADIptf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 96 -HHfnsfdkvrslpllLSQAGVRTGIIGKKH-VGPETVYPFDfaYTEEngsvlqVGRNITRiKL--LVRKflqtQDDRPF 171
Cdd:cd16032 82 aHY-------------LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE------VAFKAVQ-KLydLARG----EDGRPF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 172 FLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwtpqayDPLDVLVPYFVPNTPAARadlAAQYTTVGRMDQGVG 251
Cdd:cd16032 136 FLTVSFTHPH----------------------------------DPYVIPQEYWDLYVRRAR---RAYYGMVSYVDDKVG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 252 LVLQELRDAGVLNDTLVIFTSDN-------GIPFpsgRTNLYWPGTAEPLLVSSPE--HPKRwgqVSEAyVSLLDLTPTI 322
Cdd:cd16032 179 QLLDTLERTGLADDTIVIFTSDHgdmlgerGLWY---KMSFFEGSARVPLIISAPGrfAPRR---VAEP-VSLVDLLPTL 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506919 323 LDWFSIPYPSYAifgsktIHLTGRSLLPALE-AEPLWATVFGSQSHHEVTMSyPMRSVQHRHFRLVH 388
Cdd:cd16032 252 VDLAGGGTAPHV------PPLDGRSLLPLLEgGDSGGEDEVISEYLAEGAVA-PCVMIRRGRWKFIY 311
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-385 |
3.63e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 137.73 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGmyglhqdVHHFNSFD 102
Cdd:cd16151 2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY-------VVFGYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETVYP-------FD-------------------FAYTEENGSVLQVGRNITRIK 156
Cdd:cd16151 74 KQKTFGHLLKDAGYATAIAGKWQLGGGRGDGdyphefgFDeyclwqltetgekysrpatPTFNIRNGKLLETTEGDYGPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 157 LLVRK---FLQTQDDRPFFLY---VAFHDPHrcghsqpqYGTfcekfgngesgmgriPD---WTPQAYDPLDVLvPYFvp 227
Cdd:cd16151 154 LFADFlidFIERNKDQPFFAYypmVLVHDPF--------VPT---------------PDspdWDPDDKRKKDDP-EYF-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 228 ntpaarADLAAqYttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP-SGRTN----------LYWPGTAEPLLV 296
Cdd:cd16151 208 ------PDMVA-Y-----MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNgrevrggkgkTTDAGTHVPLIV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 297 SSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPsyaifgsKTIHLTGRSLLPALEAEP----LWATVFGSQSHHEVTM 372
Cdd:cd16151 276 NWPGLIPA-GGVSDDLVDFSDFLPTLAELAGAPLP-------EDYPLDGRSFAPQLLGKTgsprREWIYWYYRNPHKKFG 347
|
410
....*....|...
gi 4506919 373 SYPMRSVQHRHFR 385
Cdd:cd16151 348 SRFVRTKRYKLYA 360
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-350 |
4.88e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 134.60 E-value: 4.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLpqhqngmYGLHQDVHHFNSFDKVRSLPLLLSQAGVR 117
Cdd:cd16148 17 GCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGL-------YPFYHGVWGGPLEPDDPTLAEILRKAGYY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 118 TGIIGkKHVGPETVYPFDFAYTEENGSVLQVGRNI----TRIKLLVRKFL----QTQDDRPFFLYVAFHDPHrcghsqpq 189
Cdd:cd16148 90 TAAVS-SNPHLFGGPGFDRGFDTFEDFRGQEGDPGeegdERAERVTDRALewldRNADDDPFFLFLHYFDPH-------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 190 ygtfcekfgngesgmgripdwTPQAYDpldvlvpyfvpntpaarADLAaqyttvgRMDQGVGLVLQELRDAGVLNDTLVI 269
Cdd:cd16148 161 ---------------------EPYLYD-----------------AEVR-------YVDEQIGRLLDKLKELGLLEDTLVI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 270 FTSDNGIPF------PSGRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSIPYPSYaifgsktihL 343
Cdd:cd16148 196 VTSDHGEEFgehglyWGHGSNLYDEQLHVPLIIRWPGKEP--GKRVDALVSHIDIAPTLLDLLGVEPPDY---------S 264
|
....*..
gi 4506919 344 TGRSLLP 350
Cdd:cd16148 265 DGRSLLP 271
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
23-478 |
5.80e-36 |
|
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: 138.93 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 23 RNALLLLADDGGFE-SGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY--GLHQDVHHfn 99
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwnGTPLDARH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 sfdkvRSLPLLLSQAGVRTGIIGKKHVGPetvypfDFAYTEENGSVL----------QVGRNITRIK--------LLVR- 160
Cdd:cd16028 79 -----LTLALELRKAGYDPALFGYTDTSP------DPRGLAPLDPRLlsyelampgfDPVDRLDEYPaedsdtafLTDRa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 161 -KFLQTQDDRPFFLYVAFHDPH----------------------RCGHSQ------PQYGTFCEKFGNGESGMGRIPDWT 211
Cdd:cd16028 148 iEYLDERQDEPWFLHLSYIRPHppfvapapyhalydpadvpppiRAESLAaeaaqhPLLAAFLERIESLSFSPGAANAAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 212 PqaydpldvlvpyfvpnTPAARADLAAQYT-TVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP---SGRTNLYW 287
Cdd:cd16028 228 L----------------DDEEVAQMRATYLgLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGdhwLWGKDGFF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 288 PGTAE-PLLVSSPEHPKR--WGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHLTGRSLLPALEAE--PLWATvf 362
Cdd:cd16028 292 DQAYRvPLIVRDPRREADatRGQVVDAFTESVDVMPTILDWLGGEIPH---------QCDGRSLLPLLAGAqpSDWRD-- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 363 gsqshhEVTMSYPMRSVQHRHFRLVHNL-----NFKMPFpiDQDF-YVspTFQDLlnrttagqptgwykdlrhyyyraRW 436
Cdd:cd16028 361 ------AVHYEYDFRDVSTRRPQEALGLspdecSLAVIR--DERWkYV--HFAAL-----------------------PP 407
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 4506919 437 ELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWETHDP 478
Cdd:cd16028 408 LLFDLKNDPGELRDLAADPAYAAVVLRYAQKLLSWRMRHADR 449
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
21-470 |
1.90e-35 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 137.88 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfN 99
Cdd:PRK13759 6 KP-NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKVRSLPLLLSQAGVRTGIIGKKHVGPETV--------------------YPFDFAYTEENGSVLQ---VGRNITRIK 156
Cdd:PRK13759 81 PWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNllgfhnvllhdgylhsgrneDKSQFDFVSDYLAWLRekaPGKDPDLTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 157 LLVR--------------------------KFLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGRIPD 209
Cdd:PRK13759 161 IGWDcnswvarpwdleerlhptnwvgsesiEFLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 210 WT------PQAYDPldvLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-------- 275
Cdd:PRK13759 238 WEyaedqdPEGGSI---DALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHGdmlgdhyl 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 276 ------------IPFPsgrtnLYWPGTAepllvsspEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktiHL 343
Cdd:PRK13759 315 frkgypyegsahIPFI-----IYDPGGL--------LAGNR-GTVIDQVVELRDIMPTLLDLAGGTIPD---------DV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 344 TGRSLLPALEA-EPLWATVFgsqsHHEvtmsypmrsvqhrHFrlvhnlnfkmpfpidqdfyvsptfqdllnrtTAGQPTG 422
Cdd:PRK13759 372 DGRSLKNLIFGqYEGWRPYL----HGE-------------HA-------------------------------LGYSSDN 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 4506919 423 WYKDLRHYY----YRARWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAK 470
Cdd:PRK13759 404 YLTDGKWKYiwfsQTGEEQLFDLKKDPHELHNLSPSEKYQPRLREMRKKLVD 455
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-350 |
2.40e-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: 293768 [Multi-domain] Cd Length: 257 Bit Score: 132.36 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGM-----YGLHQDVHH 97
Cdd:cd16149 2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 98 FNSFDKVR-SLPLLLSQAGVRTGIIGKKHVGPETVypfDFAYTEEngsvlqvgrnitrikllvrkflqtQDDRPFFLYVA 176
Cdd:cd16149 82 PEGYLEGQtTLPEVLQDAGYRCGLSGKWHLGDDAA---DFLRRRA------------------------EAEKPFFLSVN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 177 FHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQE 256
Cdd:cd16149 135 YTAPH-----------------------------SPWGY------------------------FAAVTGVDRNVGRLLDE 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 257 LRDAGVLNDTLVIFTSDNGipFPSG------------RTNLYWPGTAEPLLVSSPEHpKRWGQVSEAYVSLLDLTPTILD 324
Cdd:cd16149 162 LEELGLTENTLVIFTSDNG--FNMGhhgiwgkgngtfPLNMYDNSVKVPFIIRWPGV-VPAGRVVDSLVSAYDFFPTLLE 238
|
330 340
....*....|....*....|....*.
gi 4506919 325 WFSIPYPSyaifgskTIHLTGRSLLP 350
Cdd:cd16149 239 LAGVDPPA-------DPRLPGRSFAD 257
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-452 |
1.12e-33 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 131.17 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGF-ESGAYN-NSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-------LPQHQNGMYGLHQd 94
Cdd:cd16143 2 NIVIILADDLGYgDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwrsrLKGGVLGGFSPPL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 95 vhhfnsFDKVR-SLPLLLSQAGVRTGIIGKKHVG----------PETVYPFDFAYTE-------ENG-------SVLQVG 149
Cdd:cd16143 81 ------IEPDRvTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkAATGTGKDVDYSKpikggplDHGfdyyfgiPASEVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 150 RNITRiKllVRKFLQTQ--DDRPFFLYVAFHDPHrcGHSQPqygtfCEKFgNGESGMGripdwtpqaydpldvlvpyfvp 227
Cdd:cd16143 155 PTLTD-K--AVEFIDQHakKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAG---------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 228 ntpaARADLAAQyttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRTNL---YWP--------------G 289
Cdd:cd16143 202 ----PYGDFVYE------LDWVVGRILDALKELGLAENTLVIFTSDNGpSPYADYKELEkfgHDPsgplrgmkadiyegG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 290 TAEPLLVSSPEH-PKrwGQVSEAYVSLLDLTPTILDWFSIPYPsyaifgsKTIHLTGRSLLPALEAEplwatvfgsqshh 368
Cdd:cd16143 272 HRVPFIVRWPGKiPA--GSVSDQLVSLTDLFATLAAIVGQKLP-------DNAAEDSFSFLPALLGP------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 369 evtmsypmrSVQHRHFRLVHNLN----------FKMpfpIDQDFyvSPTFQDLLNRTTAGQPTGwykdlrhyyyrarwEL 438
Cdd:cd16143 330 ---------KKQEVRESLVHHSGngsfairkgdWKL---IDGTG--SGGFSYPRGKEKLGLPPG--------------QL 381
|
490
....*....|....
gi 4506919 439 YDRSRDPHETQNLA 452
Cdd:cd16143 382 YNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-451 |
1.90e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 130.77 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV 95
Cdd:cd16034 1 KP-NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGndvpLPPDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 96 HhfnSFDKVrslpllLSQAGVRTGIIGKKHV-GPETVYP--------------FDF------------AYTEENGSVLQV 148
Cdd:cd16034 80 P---TIADV------LKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 149 GRNITRIKL--LVRKFL--QTQDDRPFFLYVAFHDPHrcghsqPQYGTFCEKFGNGesgmgripdwtpqaYDPLDVLVPY 224
Cdd:cd16034 151 IKGYSPDAEtdLAIEYLenQADKDKPFALVLSWNPPH------DPYTTAPEEYLDM--------------YDPKKLLLRP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 225 FVPNTPAARADLAAQ----YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS-GRT--NLYWPGTAE-PLLV 296
Cdd:cd16034 211 NVPEDKKEEAGLREDlrgyYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGShGLMnkQVPYEESIRvPFII 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 297 SSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSyaifgskTIHltGRSLLPALEAEplwatvfGSQSHHEVTMSYpm 376
Cdd:cd16034 291 RYPGKIKA-GRVVDLLINTVDIMPTLLGLCGLPIPD-------TVE--GRDLSPLLLGG-------KDDEPDSVLLQC-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 377 rsvqhrhfrlvhnlnfkmPFPIDQDFYvsptfqdllnrttagQPTGWYKDLR--HYYY----RARWELYDRSRDPHETQN 450
Cdd:cd16034 352 ------------------FVPFGGGSA---------------RDGGEWRGVRtdRYTYvrdkNGPWLLFDNEKDPYQLNN 398
|
.
gi 4506919 451 L 451
Cdd:cd16034 399 L 399
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-352 |
2.29e-31 |
|
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: 126.04 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNS 100
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA--HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 101 F----------DKVRSLPLLLSQAGVRTGIIGKKHVGPETVY-P----FDFAYTEENGSV-----------------LQV 148
Cdd:cd16157 79 YtpqnivggipDSEILLPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 149 GR--------------NITRIkLLVR--KFLQTQ--DDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMGRIPDw 210
Cdd:cd16157 159 GRyyeefkidkktgesNLTQI-YLQEalEFIEKQhdAQKPFFLYWAPDATH-----APVYAS--KPFL-GTSQRGLYGD- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 211 tpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-------------P 277
Cdd:cd16157 229 -------------------------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngP 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506919 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSYAIfgsktihLTGRSLLPAL 352
Cdd:cd16157 278 FLCGKQTTFEGGMREPAIAWWPGHIKP-GQVSHQLGSLMDLFTTSLALAGLPIPSDRA-------IDGIDLLPVL 344
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
22-347 |
5.99e-29 |
|
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: 117.96 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 22 PRNALLLLADDGGFESGAYNN--SAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHFN 99
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMT-------GRLGLRNGVGHNF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKVRSLPL-------LLSQAGVRTGIIGKKHVGPETVY-P----FDFAY--TEENGSVLQvgrniTRIKLLVRKFLQ- 164
Cdd:cd16161 74 LPTSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDYYFgiPFSHDSSLA-----DRYAQFATDFIQr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 165 -TQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDPLdvlvpyfVPNTPAARADLAAqytTV 243
Cdd:cd16161 149 aSAKDRPFFLYAALAHVH-----------------------------VPLANLPR-------FQSPTSGRGPYGD---AL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 244 GRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG--------IPFPSG---RTNLYWP---------GTAEPLLVSSPEHPK 303
Cdd:cd16161 190 QEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTgdwQGNLGGSvakastwegGHREPAIVYWPGRIP 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 4506919 304 RwGQVSEAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIH--LTGRS 347
Cdd:cd16161 270 A-NSTSAALVSTLDIFPTVVALAGASLPPGRIYDGKDLSpvLFGGS 314
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
24-325 |
2.08e-28 |
|
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: 116.50 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFESGAYNNSA-IATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYglhqdvhHFNSFD 102
Cdd:cd16029 2 HIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQ-------HGVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRS--------LPLLLSQAGVRTGIIGKKHVG--------------------------------PETVYPFDFAYTEEN 142
Cdd:cd16029 74 GEPYglplnetlLPQYLKELGYATHLVGKWHLGfytweytptnrgfdsfygyyggaedyythtsgGANDYGNDDLRDNEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 143 GSVLQVGRNITriKLLVR---KFLQTQD-DRPFFLYVAFHDPHrcghsqpqygtfcekFGNGEsgmgripdwtPQAYDPL 218
Cdd:cd16029 154 PAWDYNGTYST--DLFTDravDIIENHDpSKPLFLYLAFQAVH---------------APLQV----------PPEYADP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 219 DVLVPYFVPNTpaARADLAAqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRT--N---------LYW 287
Cdd:cd16029 207 YEDKFAHIKDE--DRRTYAA---MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsNyplrggkntLWE 281
|
330 340 350
....*....|....*....|....*....|....*...
gi 4506919 288 PGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTPTILDW 325
Cdd:cd16029 282 GGVRVPAFVWSPLLPPKRGTVSDGLMHVTDWLPTLLSL 319
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-452 |
2.80e-28 |
|
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: 115.71 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGF-ESGAYNNSAI---ATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTG---------LPQHQNGMYG 90
Cdd:cd16142 2 NILVILGDDIGWgDLGCYGGGIGrgaPTPNIDRLAKEGLRFTS-FYVEPSCTPGRAAFITGrhpirtgltTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 91 LHqdvhhfnsfDKVRSLPLLLSQAGVRTGIIGKKHVG--PE---TVYPFD----FAYT---EEngsvlQVGRNITRIKll 158
Cdd:cd16142 81 LP---------PWEPTLAELLKDAGYATAQFGKWHLGdeDGrlpTDHGFDefygNLYHtidEE-----IVDKAIDFIK-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 159 vRkflQTQDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgMGRIPDWTPQAydplDVLVpyfvpntpaaradlaa 238
Cdd:cd16142 145 -R---NAKADKPFFLYVNFTKMHFPTLPSPEF-------------EGKSSGKGKYA----DSMV---------------- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 239 qyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG---IPFP-SGRTNL------------------YWPGTAEPllv 296
Cdd:cd16142 188 ------ELDDHVGQILDALDELGIADNTIVIFTTDNGpeqDVWPdGGYTPFrgekgttweggvrvpaivRWPGKIKP--- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 297 sspehpkrwGQVSEAYVSLLDLTPTILDWFSIPYPSyAIFGSKTIHLTGRSLLPALEAEplwatvfGSQSHHEV----TM 372
Cdd:cd16142 259 ---------GRVSNEIVSHLDWFPTLAALAGAPDPK-DKLLGKDRHIDGVDQSPFLLGK-------SEKSRRSEffyfGE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 373 SYPMrSVQHRhfrlvhnlNFKMPFpidqdfyvsptfqdllnrtTAGQPTGWykDLRHYYYRARW-ELYDRSRDPHETQNL 451
Cdd:cd16142 322 GELG-AVRWK--------NWKVHF-------------------KAQEDTGG--PTGEPFYVLTFpLIFNLRRDPKERYDV 371
|
.
gi 4506919 452 A 452
Cdd:cd16142 372 T 372
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
22-497 |
7.28e-27 |
|
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: 113.31 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNS 100
Cdd:cd16158 1 PPNIVLLFADDLGYgDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVY---PGVFYPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 101 FDkvrSLPL-------LLSQAGVRTGIIGKKH--VGPETVY-P----FDF----AYTEENG------------------- 143
Cdd:cd16158 78 RG---GLPLnettiaeVLKTVGYQTAMVGKWHlgVGLNGTYlPthqgFDHylgiPYSHDQGpcqnltcfppnipcfggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 144 ------------SVLQVGRNITRIKLLVRKFLQ------TQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGNgESGMG 205
Cdd:cd16158 155 qgevpcplfyneSIVQQPVDLLTLEERYAKFAKdfiadnAKEGKPFFLYYASHHTH-----YPQFAG--QKFAG-RSSRG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 206 RIPDwtpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPS----- 280
Cdd:cd16158 227 PFGD--------------------------------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG---PStmrks 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 281 ----------GRTNLYWPGTAEPLLVSSPEHPKRwgQVSEAYVSLLDLTPTILDWFSIPYPSyaifgsktIHLTGRSLLP 350
Cdd:cd16158 272 rggnagllkcGKGTTYEGGVREPAIAYWPGRIKP--GVTHELASTLDILPTIAKLAGAPLPN--------VTLDGVDMSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 351 ALeaeplwatvFGS-QSHHEVTMSYPMRSVQHRHFRLVHNLNFKMPFpIDQDFYVSPTFQD----LLNRTTAGQPTgwyk 425
Cdd:cd16158 342 IL---------FEQgKSPRQTFFYYPTSPDPDKGVFAVRWGKYKAHF-YTQGAAHSGTTPDkdchPSAELTSHDPP---- 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506919 426 dlrhyyyrarwELYDRSRDPHETQNLATDPRFAQLLEMLrdQLAKWQWETHDPWvcAPDGV---LEEKLSPQCQP 497
Cdd:cd16158 408 -----------LLFDLSQDPSENYNLLGLPEYNQVLKQI--QQVKERFEASMKF--GESEInkgEDPALEPCCKP 467
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-348 |
1.29e-25 |
|
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: 106.31 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFESGAYNNSAIA-----------TPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGL- 91
Cdd:cd16153 3 NILWIITDDQRVDSLSCYNNAHTgksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 92 --HQDVHHFNsfdkvRSLPLLLSQAGVRTGIIGKKHVGPETVYpfdfayteengsvlqVGRNITRIKLLVRKFLQTQD-D 168
Cdd:cd16153 83 aaHPALDHGL-----PTFPEVLKKAGYQTASFGKSHLEAFQRY---------------LKNANQSYKSFWGKIAKGADsD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 169 RPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPqaydpldVLVpyfvpntPAARADLAAQYTTVGRMDQ 248
Cdd:cd16153 143 KPFFVRLSFLQPH-----------------------------TP-------VLP-------PKEFRDRFDYYAFCAYGDA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 249 GVGLVLQELRDAGVLND---TLVIFTSD-------NGIPFPSGrtnlYWPGTAE-PLLVSSPEH-PKRWGQVSEAYVSLL 316
Cdd:cd16153 180 QVGRAVEAFKAYSLKQDrdyTIVYVTGDhgwhlgeQGILAKFT----FWPQSHRvPLIVVSSDKlKAPAGKVRHDFVEFV 255
|
330 340 350
....*....|....*....|....*....|..
gi 4506919 317 DLTPTILDWFSIPYPSYAifgsktiHLTGRSL 348
Cdd:cd16153 256 DLAPTLLAAAGVDVDAPD-------YLDGRDL 280
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-356 |
7.39e-24 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 101.90 E-value: 7.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 48 PHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhqDVHHFNSF----DKVRSLPLLLSQAGVRTGIIGK 123
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT----DTLGSPMQpllsPDVPTLGHMLRAAGYYTAYKGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 124 KHV--GPETVYPFDFAYTEEngsvlqvgrnitRIKLLVRKFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgnge 201
Cdd:cd16035 103 WHLsgAAGGGYKRDPGIAAQ------------AVEWLRERGAKNADGKPWFLVVSLVNPH-------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 202 sgmgripdwtpqaydplDVLvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------ 275
Cdd:cd16035 151 -----------------DIM--FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGemggah 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 276 ----IPFpsgrtNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLLDLTPTILDWFSIPYPSYAifgSKTIHLTGRSLLPA 351
Cdd:cd16035 212 glrgKGF-----NAYEEALHVPLIISHPDLFGT-GQTTDALTSHIDLLPTLLGLAGVDAEARA---TEAPPLPGRDLSPL 282
|
....*
gi 4506919 352 LEAEP 356
Cdd:cd16035 283 LTDAD 287
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-324 |
5.76e-23 |
|
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: 101.35 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16160 3 NIVLFFADDMGYgDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 103 KVRS---LPLLLSQAGVRTGIIGKKHVG------------PE--------TVYPFDFAY----TEE-------NGSVLQV 148
Cdd:cd16160 83 LPKTevtMAEALKEAGYTTGMVGKWHLGinennhsdgahlPShhgfdfvgTNLPFTNSWacddTGRhvdfpdrSACFLYY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 149 GRNIT-----------RIKLLVRKFLQTQDDRPFFLYVAFhdphrcghSQPQYGTFCEKFGNGESGMGRIPDwtpqaydp 217
Cdd:cd16160 163 NDTIVeqpiqhehlteTLVGDAKSFIEDNQENPFFLYFSF--------PQTHTPLFASKRFKGKSKRGRYGD-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 218 ldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI------------PFPSGRTN- 284
Cdd:cd16160 227 ------------------------NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPhveycleggstgGLKGGKGNs 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 4506919 285 ----------LYWPGTAEPllvsspehpkrwgQVSEAYVSLLDLTPTILD 324
Cdd:cd16160 283 weggirvpfiAYWPGTIKP-------------RVSHEVVSTMDIFPTFVD 319
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-324 |
2.70e-20 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 92.41 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 24 NALLLLADDGGFESGA---YNNSAIATPHLDALARRSLLFRNAFtSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHF-- 98
Cdd:cd16154 2 NILLIIADDQGLDSSAqysLSSDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILT-------GKYGFRTGVLAVpd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 99 NSFDKVRSLPLLL----SQAGVRTGIIGKKHVG------PETVYPFDFA---------YTE----ENGSVLQVGR-NITR 154
Cdd:cd16154 74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGgndnspNNPGGIPYYAgilgggvqdYYNwnltNNGQTTNSTEyATTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 155 IKLLVRKFLQTQdDRPFFLYVAFHDPHRCGHSQPqygtfcekfgNGESGMGRIPDWTPQAYDPLdvlvPYFvpntpaara 234
Cdd:cd16154 154 LTNLAIDWIDQQ-TKPWFLWLAYNAPHTPFHLPP----------AELHSRSLLGDSADIEANPR----PYY--------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 235 dLAAqyttVGRMDQGVGLVLQELrDAGVLNDTLVIFTSDNGIP-------FPSGRT--NLYWPGTAEPLLVSSPEHPkRW 305
Cdd:cd16154 210 -LAA----IEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTPgqvvdlpYTRNHAkgSLYEGGINVPLIVSGAGVE-RA 282
|
330
....*....|....*....
gi 4506919 306 GQVSEAYVSLLDLTPTILD 324
Cdd:cd16154 283 NERESALVNATDLYATIAE 301
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
23-324 |
6.30e-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: 85.94 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 23 RNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFR-NAFTSVSSCSPSRASLLTGLPQHQNGMYG--------LH 92
Cdd:cd00016 1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYTGngsadpelPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 93 QDVHHFNSFDkvrSLPLLLSQAGVRTGIIGkkhvgpetvypfdfayteengsvlqvgrnitrikllVRKFL-QTQDDRPF 171
Cdd:cd00016 81 RAAGKDEDGP---TIPELLKQAGYRTGVIG------------------------------------LLKAIdETSKEKPF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 172 FLYVAFHDPHRCGHSqpqygtfcekfgngesgmgriPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVG 251
Cdd:cd00016 122 VLFLHFDGPDGPGHA---------------------YGPNTPEY------------------------YDAVEEIDERIG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 252 LVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRT--NLYWPGTAE-----PLLVSSPEHPKrwGQVSEAYVSLLDLTPTIL 323
Cdd:cd00016 157 KVLDALKKAGDADDTVIIVTADHGgIDKGHGGDpkADGKADKSHtgmrvPFIAYGPGVKK--GGVKHELISQYDIAPTLA 234
|
.
gi 4506919 324 D 324
Cdd:cd00016 235 D 235
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
21-353 |
7.35e-16 |
|
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: 80.02 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 21 RPrNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMyGLHQDVHHFN 99
Cdd:cd16159 1 KP-NIVLFMADDLGIgDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGM-ASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 100 SFDKVRSLP-------LLLSQAGVRTGIIGKKHVG--PETV---------YPFDFAY-----------TEENGSVLQVGR 150
Cdd:cd16159 79 FTASSGGLPpnettfaEVLKQQGYSTALIGKWHLGlhCESRndfchhplnHGFDYFYglpltnlkdcgDGSNGEYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 151 N-----------------------------------------------ITRIK----LLVR------------------- 160
Cdd:cd16159 159 PlfplltafvlitaltiflllylgavskrffvfllilsllfislffllLITNRyfncILMRnhevveqpmslenltqrlt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 161 ----KFLQTQDDRPFFLYVAFHDPHRcghsqpqyGTFCEKFGNGESGMGRIPDwtpqaydpldvlvpyfvpntpaaradl 236
Cdd:cd16159 239 keaiSFLERNKERPFLLVMSFLHVHT--------ALFTSKKFKGRSKHGRYGD--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 237 aaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-----------------IPFPSGRTNLYWPGTAEPLLVSSP 299
Cdd:cd16159 284 -----NVEEMDWSVGQILDALDELGLKDNTFVYFTSDNGghleeisvggeygggngGIYGGKKMGGWEGGIRVPTIVRWP 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 4506919 300 EHPKRWGQVSEAyVSLLDLTPTILDWFSIPYPSyaifgskTIHLTGRSLLPALE 353
Cdd:cd16159 359 GVIPPGSVIDEP-TSLMDIFPTVAALAGAPLPS-------DRIIDGRDLMPLLT 404
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
33-337 |
1.38e-15 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 79.31 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 33 GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLP-QHQNGMYGLHQDVHHFnsfdkvrSLPLLL 111
Cdd:COG1368 246 SDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRPGQNNFP-------SLPSIL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 112 SQAGVRTGIIgkkHVGPET------VYP---FDFAYTEENgsvLQVGRNIT-RI--KLLVRKFLQT--QDDRPFFLYV-- 175
Cdd:COG1368 319 KKQGYETSFF---HGGDGSfwnrdsFYKnlgFDEFYDRED---FDDPFDGGwGVsdEDLFDKALEEleKLKKPFFAFLit 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 176 -AFHDPhrcghsqpqYgtfceKFGNGESGMGRIPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVL 254
Cdd:COG1368 393 lSNHGP---------Y-----TLPEEDKKIPDYGKTTLNNY------------------------LNAVRYADQALGEFI 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 255 QELRDAGVLNDTLVIFTSDNGIPFPsGRTNLYWPGTAE--PLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSIPYPS 332
Cdd:COG1368 435 EKLKKSGWYDNTIFVIYGDHGPRSP-GKTDYENPLERYrvPLLIYSPGLKK--PKVIDTVGSQIDIAPTLLDLLGIDYPS 511
|
....*
gi 4506919 333 YAIFG 337
Cdd:COG1368 512 YYAFG 516
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
42-354 |
1.11e-13 |
|
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: 72.57 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 42 NSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHqngmygLHQDVHHFNSFDK-VRSLPLLLSQAGVRTGI 120
Cdd:cd16171 21 NQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYKGLDPnYPTWMDRLEKHGYHTQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 121 IGKKHV--GPETVYPFDFAYTEENGSVL-QVGR---NITRIKLLVRKFL---QTQD-------------DRPFFLYVAFH 178
Cdd:cd16171 95 YGKLDYtsGHHSVSNRVEAWTRDVPFLLrQEGRptvNLVGDRSTVRVMLkdwQNTDkavhwirkeapnlTQPFALYLGLN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 179 DPHrcghsqpQYGTfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELR 258
Cdd:cd16171 175 LPH-------PYPS------------------------------PSMGENFGSIRNIRAFYYAMCAETDAMLGEIISALK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 259 DAGVLNDTLVIFTSDNGIPFPSGR----TNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWFSIPYPSya 334
Cdd:cd16171 218 DTGLLDKTYVFFTSDHGELAMEHRqfykMSMYEGSSHVPLLIMGPGIKA--GQQVSDVVSLVDIYPTMLDIAGVPQPQ-- 293
|
330 340
....*....|....*....|
gi 4506919 335 ifgsktiHLTGRSLLPALEA 354
Cdd:cd16171 294 -------NLSGYSLLPLLSE 306
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-326 |
4.23e-11 |
|
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: 63.47 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRA--SLLTGLPQHQNGMYGLHQDVHHfnsfdKVRSLPLLLSQAG 115
Cdd:cd16015 17 DKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN-----PLPSLPSILKEQG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 116 VRTGIIgkkHVGP------ETVYP---FDFAYTEENGSVLQVGRNITRI--KLLVRKF---LQTQDDRPFFLYV---AFH 178
Cdd:cd16015 92 YETIFI---HGGDasfynrDSVYPnlgFDEFYDLEDFPDDEKETNGWGVsdESLFDQAleeLEELKKKPFFIFLvtmSNH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 179 DPhrcghsqpqYGTFCEKFgngesgmgripdwtpqaydpldvlvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELR 258
Cdd:cd16015 169 GP---------YDLPEEKK--------------------------DEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLK 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506919 259 DAGVLNDTLVIFTSD---NGIPFPSGRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLLDLTPTILDWF 326
Cdd:cd16015 214 KSGLYENTIIVIYGDhlpSLGSDYDETDEDPLDLYRTPLLIYSPGLKK--PKKIDRVGSQIDIAPTLLDLL 282
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
10-276 |
5.17e-11 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 64.38 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 10 ALLLVLGLCRARPRNALLLLADdgGFesGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCS-PSRASLLTGLP--QHQ- 85
Cdd:COG1524 11 SLLAAAAAAAPPAKKVVLILVD--GL--RADLLERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYpgEHGi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 86 --NGMY-----------GLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIG-KKHVGPETV-YPFDFAYteeNGSVLQVGR 150
Cdd:COG1524 87 vgNGWYdpelgrvvnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFwPSFEGSGLIdAARPYPY---DGRKPLLGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 151 NITRiKLLVRKFLQT-QDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNT 229
Cdd:COG1524 164 PAAD-RWIAAAALELlREGRPDLLLVYLPDLDYAGH---RYG-----------------------------------PDS 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 4506919 230 PAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:COG1524 205 PEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| DUF4976 |
pfam16347 |
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around ... |
424-477 |
1.79e-08 |
|
Domain of unknown function (DUF4976); This family consists of uncharacterized proteins around 530 residues in length and is mainly found in various Bacteroides species. Several proteins in this family are annotated as Arylsulfatases, but the function of this protein is unknown.
Pssm-ID: 406689 [Multi-domain] Cd Length: 103 Bit Score: 52.25 E-value: 1.79e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 4506919 424 YKdLRHYYYRAR-WELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWETHD 477
Cdd:pfam16347 50 YK-LIHFYNDIDeWELYDLQKDPKEMNNVYGDPEYAEVQAELKEELEELRKQYKD 103
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
26-276 |
4.37e-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: 54.51 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 26 LLLLADdgGFESgAYNNSAIATPHLDALARRSLLF---RNAFTSVSScsPSRASLLTGLP--QHQ---NGMY-------G 90
Cdd:cd16018 4 IVISID--GFRW-DYLDRAGLTPNLKRLAEEGVRAkyvKPVFPTLTF--PNHYSIVTGLYpeSHGivgNYFYdpktneeF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 91 LHQDVHHFNSFDKVRSLPLLLSQAGVRTGII------GKKHVGPETVYPFDFAYTEENGSVLqvgrNITRIKLLVRKFlq 164
Cdd:cd16018 79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYfwpgseVAIIGYNPTPIPLGGYWQPYNDSFP----FEERVDTILEWL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 165 tQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvg 244
Cdd:cd16018 153 -DLERPDLILLYFEEPDSAGH---KYG-----------------------------------PDSPEVNEALK------- 186
|
250 260 270
....*....|....*....|....*....|..
gi 4506919 245 RMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:cd16018 187 RVDRRLGYLIEALKERGLLDDTNIIVVSDHGM 218
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
47-276 |
5.90e-08 |
|
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.
Pssm-ID: 396300 [Multi-domain] Cd Length: 343 Bit Score: 54.73 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 47 TPHLDALARRSLLFRNAFTSV-SSCSPSRASLLTGLPQHQNGMYG-----------LHQDVHHFNSFDKVRSLPLL--LS 112
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpktgeyLVFVISDPEDPRWWQGEPIWdtAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 113 QAGVRTGII----GKKHVGPETVYPFDFAYTEENGSVLQVGR--NITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHs 186
Cdd:pfam01663 100 KAGVRAAALfwpgSEVDYSTYYGTPPRYLKDDYNNSVPFEDRvdTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGH- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506919 187 qpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDT 266
Cdd:pfam01663 179 --RYG-----------------------------------PDSPEVEDALR-------RVDRAIGDLLEALDERGLFEDT 214
|
250
....*....|
gi 4506919 267 LVIFTSDNGI 276
Cdd:pfam01663 215 NVIVVSDHGM 224
|
|
| |
