|
Name |
Accession |
Description |
Interval |
E-value |
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
24-316 |
6.61e-116 |
|
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: 341.03 E-value: 6.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSFDK 103
Cdd:cd16027 2 NILWIIADDLSPDLGGYGGNVVKTPNLDRLAAEGVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRS--RGFPLPDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 104 VRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENgsvlQVGRNITRIKLLVRKFLQTQD-DRPFFLYVAFHDPHR 182
Cdd:cd16027 80 VKTLPELLREAGYYTGLIGKTHYNPDAVFPFDDEMRGPD----DGGRNAWDYASNAADFLNRAKkGQPFFLWFGFHDPHR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 183 CGHSQPQYGTFcekfgngesgmgripdwtpqaYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGV 262
Cdd:cd16027 156 PYPPGDGEEPG---------------------YDPEKVKVPPYLPDTPEVREDLADYYDEIERLDQQVGEILDELEEDGL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1209857043 263 LNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16027 215 LDNTIVIFTSDHGMPFPRAKGTLYDSGLRVPLIVRWPGKIKP-GSVSDALVSFI 267
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
21-316 |
7.63e-61 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 200.49 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFN 99
Cdd:COG3119 23 RP-NILFILADDlGYGDLGCYGNPLIKTPNIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKVrSLPLLLSQAGVRTGIIGKKHvgpetVYpFDFAYTEEngsvlqvgrnitrikllVRKFLQTQ--DDRPFFLYVAF 177
Cdd:COG3119 102 PPDEP-TLAELLKEAGYRTALFGKWH-----LY-LTDLLTDK-----------------AIDFLERQadKDKPFFLYLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 178 HDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYDPLDVLVP-YFVP---NTPAARADLAAQYTTVGRMDQGVGLV 253
Cdd:COG3119 158 NAPHAPYQAPEEY---------------------LDKYDGKDIPLPpNLAPrdlTEEELRRARAAYAAMIEEVDDQVGRL 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209857043 254 LQELRDAGVLNDTLVIFTSDNGIPFPS-----GRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:COG3119 217 LDALEELGLADNTIVVFTSDNGPSLGEhglrgGKGTLYEGGIRVPLIVRWPGKIKA-GSVSDALVSLI 283
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
24-316 |
5.95e-56 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 182.64 E-value: 5.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNsfD 102
Cdd:cd16022 2 NILLIMTDDLGYDDlGCYGNPDIKTPNLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGNGGGLP--P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRSLPLLLSQAGVRTGIIGKKHvgpetvypfDFAyteengsvlqvgrnitrikllvRKFLQTQD-DRPFFLYVAFHDPH 181
Cdd:cd16022 80 DEPTLAELLKEAGYRTALIGKWH---------DEA----------------------IDFIERRDkDKPFFLYVSFNAPH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 182 rcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQELRDAG 261
Cdd:cd16022 129 -----------------------------PPFAY------------------------YAMVSAIDDQIGRILDALEELG 155
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 262 VLNDTLVIFTSDNGIPFPSGR-----TNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16022 156 LLDNTLIVFTSDHGDMLGDHGlrgkkGSLYEGGIRVPFIVRWPGKIPA-GQVSDALVSLL 214
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
23-314 |
2.61e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 170.30 E-value: 2.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 23 RNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhfNSF 101
Cdd:pfam00884 1 PNVVLVLGESLRAPDlGLYGYPRPTTPFLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVSTPV----GLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 102 DKVRSLPLLLSQAGVRTGIIGKKHVGP-----ETVYPFDFAYTEENGSVLQVGRNITRI---------KLLVRKFLQ--T 165
Cdd:pfam00884 77 RTEPSLPDLLKRAGYNTGAIGKWHLGWynnqsPCNLGFDKFFGRNTGSDLYADPPDVPYncsgggvsdEALLDEALEflD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 166 QDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgmgripdwtPQAYdpldvlvPYFVPNTPAARADLAAQYTTVGR 245
Cdd:pfam00884 157 NNDKPFFLVLHTLGSHGPPYYPDRY---------------------PEKY-------ATFKPSSCSEEQLLNSYDNTLLY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209857043 246 MDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPF--------PSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVS 314
Cdd:pfam00884 209 TDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLgegggylhGGKYDNAPEGGYRVPLLIWSPGGKAK-GQKSEALVS 284
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
21-313 |
3.26e-48 |
|
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: 168.09 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVhhFN 99
Cdd:cd16031 1 KRPNIIFILTDDHRYDAlGCYGNPIVKTPNIDRLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPL--FD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKvrSLPLLLSQAGVRTGIIGKKHVGPETVYP---FDF------------AYTEENGSVLQVGRNITRIKL-LVRKFL 163
Cdd:cd16031 79 ASQP--TYPKLLRKAGYQTAFIGKWHLGSGGDLPppgFDYwvsfpgqgsyydPEFIENGKRVGQKGYVTDIITdKALDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 164 QTQD-DRPFFLYVAFHDPHRCGHSQPQYGtfcEKFGNGEsgMGRIPDWTPQAYDPLdvlvPYFVPNTPAARADLA----- 237
Cdd:cd16031 157 KERDkDKPFCLSLSFKAPHRPFTPAPRHR---GLYEDVT--IPEPETFDDDDYAGR----PEWAREQRNRIRGVLdgrfd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 238 ----------AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG-------RTnLYWPGTAEPLLVSSPE 300
Cdd:cd16031 228 tpekyqrymkDYLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNG--FFLGehglfdkRL-MYEESIRVPLIIRDPR 304
|
330
....*....|...
gi 1209857043 301 HPKRwGQVSEAYV 313
Cdd:cd16031 305 LIKA-GTVVDALV 316
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
21-315 |
6.62e-47 |
|
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: 164.15 E-value: 6.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGF-ESGAYNnSAIATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTGLPQHQNG---MYGLHQDVH 96
Cdd:cd16025 2 RP-NILLILADDLGFsDLGCFG-GEIPTPNLDALAAEGLRFTN-FHTTALCSPTRAALLTGRNHHQVGmgtMAELATGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 97 HFNSF--DKVRSLPLLLSQAGVRTGIIGKKHVGPETVYpFDFAYTEengsvlqvgrnitriKLLvrKFLQTQ--DDRPFF 172
Cdd:cd16025 79 GYEGYlpDSAATIAEVLKDAGYHTYMSGKWHLGPDDYY-STDDLTD---------------KAI--EYIDEQkaPDKPFF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 173 LYVAF---HDPHrcgHSQPQY-----GTFcekfgngESG--------------MGRIPDWTPQAYDPLDvlvpyfVPN-- 228
Cdd:cd16025 141 LYLAFgapHAPL---QAPKEWidkykGKY-------DAGwdalreerlerqkeLGLIPADTKLTPRPPG------VPAwd 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 229 --TPAARADL-------AAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IPFPSGRTNLYW 287
Cdd:cd16025 205 slSPEEKKLEarrmevyAAM---VEHMDQQIGRLIDYLKELGELDNTLIIFLSDNGasaepgwanasnTPFRLYKQASHE 281
|
330 340
....*....|....*....|....*...
gi 1209857043 288 PGTAEPLLVSSPEHPKRWGQVSEAYVSL 315
Cdd:cd16025 282 GGIRTPLIVSWPKGIKAKGGIRHQFAHV 309
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-316 |
2.04e-44 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 156.57 E-value: 2.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAF----TSVSSCSPSRASLLTglpqhqnGMYGLH-QD 94
Cdd:cd16155 2 KP-NILFILADDQRADTiGALGNPEIQTPNLDRLARRGTSFTNAYnmggWSGAVCVPSRAMLMT-------GRTLFHaPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 95 VHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVgpetvypfDFAyteeNGSVlqvgrnitrikllvrKFL--QTQDDRPFF 172
Cdd:cd16155 74 GGKAAIPSDDKTWPETFKKAGYRTFATGKWHN--------GFA----DAAI---------------EFLeeYKDGDKPFF 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 173 LYVAFHDPHrcghsQPQYGT--FCEKFGNGEsgmgrIPDwtPQAYDPL------------DVLVPYfvPNTPAA-RADLA 237
Cdd:cd16155 127 MYVAFTAPH-----DPRQAPpeYLDMYPPET-----IPL--PENFLPQhpfdngegtvrdEQLAPF--PRTPEAvRQHLA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 238 AQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYV 313
Cdd:cd16155 193 EYYAMITHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGShglmGKQNLYEHSMRVPLIISGPGIPK--GKRRDALV 270
|
...
gi 1209857043 314 SLL 316
Cdd:cd16155 271 YLQ 273
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-310 |
3.69e-38 |
|
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: 141.19 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16145 2 NIIFILADDlGYGDLGCYGQKKIKTPNLDRLAAEGMRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSEPGGQDPLPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETV--YP----FDF---------------AYTEENG------SVLQVGRNITRI 155
Cdd:cd16145 82 DDVTLAEVLKKAGYATAAFGKWGLGGPGTpgHPtkqgFDYfygyldqvhahnyypEYLWRNGekvplpNNVIPPLDEGNN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 156 KLLVR-------------KFLQTQDDRPFFLYVAFHDPHrcGHSQpqygtfcekfgngesgmgrIPDWTPQAYDPLDvLV 222
Cdd:cd16145 162 AGGGGgtyshdlftdealDFIRENKDKPFFLYLAYTLPH--APLQ-------------------VPDDGPYKYKPKD-PG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 223 PYFVPNTPAARADLAAQyttVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-----------------PFPSGRTNL 285
Cdd:cd16145 220 IYAYLPWPQPEKAYAAM---VTRLDRDVGRILALLKELGIDENTLVVFTSDNGPhseggsehdpdffdsngPLRGYKRSL 296
|
330 340
....*....|....*....|....*
gi 1209857043 286 YWPGTAEPLLVSSPEHPKRwGQVSE 310
Cdd:cd16145 297 YEGGIRVPFIARWPGKIPA-GSVSD 320
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-275 |
1.33e-37 |
|
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: 139.24 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 22 PRNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-LPQ---------HQNGMYG 90
Cdd:cd16026 1 KPNIVVILADDLGYGDlGCYGSPLIKTPNIDRLAAEGVRFTDFYAAAPVCSPSRAALLTGrYPVrvglpgvvgPPGSKGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 91 LHQDVHhfnsfdkvrSLPLLLSQAGVRTGIIGKKHVG--PETvYP----FDFAY---------------TEENGSVLQVG 149
Cdd:cd16026 81 LPPDEI---------TIAEVLKKAGYRTALVGKWHLGhqPEF-LPtrhgFDEYFgipysndmwpfplyrNDPPGPLPPLM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 150 RNITRI----------KLLVRK---FLQTQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFgNGESGMGRIPDwtpqayd 216
Cdd:cd16026 151 ENEEVIeqpadqssltQRYTDEavdFIERNKDQPFFLYLAHTMPH-----VPLFAS--EKF-KGRSGAGLYGD------- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1209857043 217 pldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16026 216 -------------------------VVEELDWSVGRILDALKELGLEENTLVIFTSDNG 249
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-314 |
1.58e-37 |
|
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: 139.60 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGL--PQHQNGMYGLHQDVHHFNS 100
Cdd:cd16144 2 NIVLILVDDlGWADLGCYGSKFYETPNIDRLAKEGMRFTQAYAAAPVCSPSRASILTGQypARLGITDVIPGRRGPPDNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 101 F-----------DKVRSLPLLLSQAGVRTGIIGKKHVGPE-TVYP----FD---------------FAYTEENGSVLQVG 149
Cdd:cd16144 82 KlipppsttrlpLEEVTIAEALKDAGYATAHFGKWHLGGEgGYGPedqgFDvniggtgnggppsyyFPPGKPNPDLEDGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 150 RNITRIKLLVR---KFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQaydpldvlvpyfv 226
Cdd:cd16144 162 EGEYLTDRLTDeaiDFIEQNKDKPFFLYLSHYAVH-----------------------------TPI------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 227 pntpAARADLAAQYTTVGR-----------------MDQGVGLVLQELRDAGVLNDTLVIFTSDNG------------IP 277
Cdd:cd16144 200 ----QARPELIEKYEKKKKglrkgqknpvyaamiesLDESVGRILDALEELGLADNTLVIFTSDNGglstrggpptsnAP 275
|
330 340 350
....*....|....*....|....*....|....*..
gi 1209857043 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVS 314
Cdd:cd16144 276 LRGGKGSLYEGGIRVPLIVRWPGVIKP-GSVSDVPVI 311
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
23-316 |
4.58e-34 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 128.04 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 23 RNALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNS- 100
Cdd:cd16037 1 PNILIIMSDEhNPDAMGCYGHPVVRTPNLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWD--------NAd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 101 --FDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFdFAYTeengsvlqvgRNITRiklLVRKFLQTQ--DDRPFFLYVA 176
Cdd:cd16037 73 pyDGDVPSWGHALRAAGYETVLIGKLHFRGEDQRHG-FRYD----------RDVTE---AAVDWLREEaaDDKPWFLFVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 177 FHDPHrcghsqpqygtFcekfgngesgmgriPDWTPQA-YDpldvlvpYFVpntpaaRADLAAQYTTVGRMDQGVGLVLQ 255
Cdd:cd16037 139 FVAPH-----------F--------------PLIAPQEfYD-------LYV------RRARAAYYGLVEFLDENIGRVLD 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209857043 256 ELRDAGVLNDTLVIFTSDNGIPFPS----GRTNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16037 181 ALEELGLLDNTLIIYTSDHGDMLGErglwGKSTMYEESVRVPMIISGPGIPA--GKRVKTPVSLV 243
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
24-289 |
9.62e-34 |
|
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: 128.82 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSfd 102
Cdd:cd16146 2 NVILILTDDQGYgDLGFHGNPILKTPNLDRLAAESVRFTNFHVS-PVCAPTRAALLTGRYPFRTGVWHTILGRERMRL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRSLPLLLSQAGVRTGIIGKKHVGpeTVYP-------FDFAYTEENGSVLQVG-------------RNITRIK------ 156
Cdd:cd16146 79 DETTLAEVFKDAGYRTGIFGKWHLG--DNYPyrpqdrgFDEVLGHGGGGIGQYPdywgndyfddtyyHNGKFVKtegyct 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 157 -LLVR---KFLQTQDDRPFFLYVAFHDPHRcghsqpqygtfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAA 232
Cdd:cd16146 157 dVFFDeaiDFIEENKDKPFFAYLATNAPHG----------------------------------------PLQVPDKYLD 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209857043 233 R-------ADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipfPSGRTNLYWPG 289
Cdd:cd16146 197 PykdmgldDKLAAFYGMIENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRFNA 257
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-341 |
9.15e-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: 126.16 E-value: 9.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGF-ESGAYN-NSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTG-------LPQHQNGMYGLHQd 94
Cdd:cd16143 2 NIVIILADDLGYgDISCYNpDSKIPTPNIDRLAAEGMRFTDAHSPSSVCTPSRYGLLTGrypwrsrLKGGVLGGFSPPL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 95 vhhfnsFDKVR-SLPLLLSQAGVRTGIIGKKHVG----------PETVYPFDFAYTE-------ENG-------SVLQVG 149
Cdd:cd16143 81 ------IEPDRvTLAKMLKQAGYRTAMVGKWHLGldwkkkdgkkAATGTGKDVDYSKpikggplDHGfdyyfgiPASEVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 150 RNITRiKllVRKFLQTQ--DDRPFFLYVAFHDPHrcGHSQPqygtfCEKFgNGESGMGripdwtpqaydpldvlvpyfvp 227
Cdd:cd16143 155 PTLTD-K--AVEFIDQHakKDKPFFLYFALPAPH--TPIVP-----SPEF-QGKSGAG---------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 228 ntpaARADLAAQyttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRTNL---YWP--------------G 289
Cdd:cd16143 202 ----PYGDFVYE------LDWVVGRILDALKELGLAENTLVIFTSDNGpSPYADYKELEkfgHDPsgplrgmkadiyegG 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209857043 290 TAEPLLVSSPEH-PKrwGQVSEAYVSL----------LGTEAQrDDVAVRGVGstrHLPLLIG 341
Cdd:cd16143 272 HRVPFIVRWPGKiPA--GSVSDQLVSLtdlfatlaaiVGQKLP-DNAAEDSFS---FLPALLG 328
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-316 |
1.06e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293757 [Multi-domain] Cd Length: 411 Bit Score: 126.18 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNSF- 101
Cdd:cd16033 2 NILFIMTDQQRYDTlGCYGNPIVKTPNIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVL---NNVENAGAYs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 102 ----DKVRSLPLLLSQAGVRTGIIGKKHVGPETVyPFDFAYtEENGSVLQ------VGRNITRIkllvRKFLqtQDDRPF 171
Cdd:cd16033 79 rglpPGVETFSEDLREAGYRNGYVGKWHVGPEET-PLDYGF-DEYLPVETtieyflADRAIEML----EELA--ADDKPF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 172 FLYVAFHDPHrcghsQPqYgtfcekfgngesgmgRIPDWTPQAYDPLDVLVP--YFVP--NTPAA--------------- 232
Cdd:cd16033 151 FLRVNFWGPH-----DP-Y---------------IPPEPYLDMYDPEDIPLPesFADDfeDKPYIyrrerkrwgvdtede 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 233 ---RADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG---------------------IPFPSGrtnlyWP 288
Cdd:cd16033 210 edwKEIIAHYWGYITLIDDAIGRILDALEELGLADDTLVIFTSDHGdalgahrlwdkgpfmyeetyrIPLIIK-----WP 284
|
330 340
....*....|....*....|....*...
gi 1209857043 289 GTAEPllvsspehpkrwGQVSEAYVSLL 316
Cdd:cd16033 285 GVIAA------------GQVVDEFVSLL 300
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
21-275 |
3.37e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 124.60 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV 95
Cdd:cd16034 1 KP-NILFIFADQHRAQAlGCAGDDPVKTPNLDRLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGndvpLPPDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 96 HhfnSFDKVrslpllLSQAGVRTGIIGKKHV-GPETVYP--------------FDF------------AYTEENGSVLQV 148
Cdd:cd16034 80 P---TIADV------LKDAGYRTGYIGKWHLdGPERNDGraddytppperrhgFDYwkgyecnhdhnnPHYYDDDGKRIY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 149 GRNITRIKL--LVRKFL--QTQDDRPFFLYVAFHDPHrcghsqPQYGTFCEKFGNGesgmgripdwtpqaYDPLDVLVPY 224
Cdd:cd16034 151 IKGYSPDAEtdLAIEYLenQADKDKPFALVLSWNPPH------DPYTTAPEEYLDM--------------YDPKKLLLRP 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1209857043 225 FVPNTPAARADLAAQ----YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16034 211 NVPEDKKEEAGLREDlrgyYAMITALDDNIGRLLDALKELGLLENTIVVFTSDHG 265
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
21-314 |
9.25e-32 |
|
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: 123.43 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGFESGAYNnsaiATPHLDA-LARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDvhhFN 99
Cdd:cd16147 1 RP-NIVLILTDDQDVELGSMD----PMPKTKKlLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPP---GG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKV-------RSLPLLLSQAGVRTGIIGK------KHVGPETVYP-FDFAYTEENGSV-----LQVGRNITRIK---- 156
Cdd:cd16147 73 GYPKFwqnglerSTLPVWLQEAGYRTAYAGKylngygVPGGVSYVPPgWDEWDGLVGNSTyynytLSNGGNGKHGVsypg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 157 -----LLVRK---FLQT--QDDRPFFLYVAFHDPHRCGHSQPQYGtfcekfgNGESGMGRIPDWTPQAYDPLDVlvPYFV 226
Cdd:cd16147 153 dyltdVIANKaldFLRRaaADDKPFFLVVAPPAPHGPFTPAPRYA-------NLFPNVTAPPRPPPNNPDVSDK--PHWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 227 PNTPAARADLAAQYTTVGR--------MDQGVGLVLQELRDAGVLNDTLVIFTSDNGipF-------PSGRTNLYWPGTA 291
Cdd:cd16147 224 RRLPPLNPTQIAYIDELYRkrlrtlqsVDDLVERLVNTLEATGQLDNTYIIYTSDNG--YhlgqhrlPPGKRTPYEEDIR 301
|
330 340
....*....|....*....|...
gi 1209857043 292 EPLLVSSPEHPKrwGQVSEAYVS 314
Cdd:cd16147 302 VPLLVRGPGIPA--GVTVDQLVS 322
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-298 |
2.49e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 118.88 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGM-----YGLHQDVHH 97
Cdd:cd16149 2 NILFILTDDQGPWAlGCYGNSEAVTPNLDRLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIhdwivEGSHGKTKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 98 FNSFDKVR-SLPLLLSQAGVRTGIIGKKHVGPETVypfDFayteengsvlqvgrnitriklLVRkflQTQDDRPFFLYVA 176
Cdd:cd16149 82 PEGYLEGQtTLPEVLQDAGYRCGLSGKWHLGDDAA---DF---------------------LRR---RAEAEKPFFLSVN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 177 FHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVLQE 256
Cdd:cd16149 135 YTAPH-----------------------------SPWGY------------------------FAAVTGVDRNVGRLLDE 161
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209857043 257 LRDAGVLNDTLVIFTSDNGipFPSG------------RTNLY-----------WPGTAEPLLVSS 298
Cdd:cd16149 162 LEELGLTENTLVIFTSDNG--FNMGhhgiwgkgngtfPLNMYdnsvkvpfiirWPGVVPAGRVVD 224
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-313 |
3.42e-31 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 121.55 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGmyglhqdVHHFNSFD 102
Cdd:cd16151 2 NIILIMADDLGYECiGCYGGESYKTPNIDALAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYNFRNY-------VVFGYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRSLPLLLSQAGVRTGIIGKKHVGPETVYP-------FD-------------------FAYTEENGSVLQVGRNITRIK 156
Cdd:cd16151 74 KQKTFGHLLKDAGYATAIAGKWQLGGGRGDGdyphefgFDeyclwqltetgekysrpatPTFNIRNGKLLETTEGDYGPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 157 LLVRK---FLQTQDDRPFFLY---VAFHDPHrcghsqpqYGTfcekfgngesgmgriPD---WTPQAYDPLDVLvPYFvp 227
Cdd:cd16151 154 LFADFlidFIERNKDQPFFAYypmVLVHDPF--------VPT---------------PDspdWDPDDKRKKDDP-EYF-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 228 ntpaarADLAAqYttvgrMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFP-SGRTN----------LYWPGTAEPLLV 296
Cdd:cd16151 208 ------PDMVA-Y-----MDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPiTSRTNgrevrggkgkTTDAGTHVPLIV 275
|
330
....*....|....*..
gi 1209857043 297 SSPEHPKRwGQVSEAYV 313
Cdd:cd16151 276 NWPGLIPA-GGVSDDLV 291
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-316 |
4.28e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 113.48 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGmyglHQDVHHFNSFDKvrslPLLLS---QA 114
Cdd:cd16150 17 GHLGNPAAVTPNLDALAAEGVRFSNAYCQNPVCSPSRCSFLTGWYPHVNG----HRTLHHLLRPDE----PNLLKtlkDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 115 GVRTGIIGKKHVGPETVYPFDFAYTEEngsvLQVGRNITRIKllvrkflQTQDDRPFFLYVAFHDPHrcghsqPQYGtfC 194
Cdd:cd16150 89 GYHVAWAGKNDDLPGEFAAEAYCDSDE----ACVRTAIDWLR-------NRRPDKPFCLYLPLIFPH------PPYG--V 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 195 EKfgngesgmgriPDWTpqAYDPLDVLVPyfVPNTPAARADL-----------------------AAQYTTVGRMDQGVG 251
Cdd:cd16150 150 EE-----------PWFS--MIDREKLPPR--RPPGLRAKGKPsmlegiekqgldrwseerwrelrATYLGMVSRLDHQFG 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1209857043 252 LVLQELRDAGVLNDTLVIFTSDNGipfpsGRTNLY-----WPGTAE------PLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16150 215 RLLEALKETGLYDDTAVFFFSDHG-----DYTGDYglvekWPNTFEdcltrvPLIIKPPGGPA--GGVSDALVELV 283
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-316 |
4.67e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 110.72 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADdggfeS------GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLpqhqngmYGLHQDVHH 97
Cdd:cd16148 2 NVILIVID-----SlradhlGCYGYDRVTTPNLDRLAAEGVVFDNHYSGSNPTLPSRFSLFTGL-------YPFYHGVWG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 98 FNSFDKVRSLPLLLSQAGVRTGIIGkKHVGPETVYPFDFAYTEENGSVLQVGRNI----TRIKLLVRKFL----QTQDDR 169
Cdd:cd16148 70 GPLEPDDPTLAEILRKAGYYTAAVS-SNPHLFGGPGFDRGFDTFEDFRGQEGDPGeegdERAERVTDRALewldRNADDD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 170 PFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDpldvlvpyfvpntpaarADLAaqyttvgRMDQG 249
Cdd:cd16148 149 PFFLFLHYFDPH-----------------------------EPYLYD-----------------AEVR-------YVDEQ 175
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1209857043 250 VGLVLQELRDAGVLNDTLVIFTSDNGIPFpsGRTNLYW----PGTAE----PLLVSSPEHPKrwGQVSEAYVSLL 316
Cdd:cd16148 176 IGRLLDKLKELGLLEDTLVIVTSDHGEEF--GEHGLYWghgsNLYDEqlhvPLIIRWPGKEP--GKRVDALVSHI 246
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
24-313 |
7.84e-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: 112.26 E-value: 7.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFESGAYNNSA-IATPHLDALARRSLLFRNAFTSvSSCSPSRASLLTGLPQHQNGMYglHQDVHHfnsfD 102
Cdd:cd16029 2 HIVFILADDLGWNDVGFHGSDqIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYPIHTGMQ--HGVILA----G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRSLPL-------LLSQAGVRTGIIGKKHVG--------------------------------PETVYPFDFAYTEENG 143
Cdd:cd16029 75 EPYGLPLnetllpqYLKELGYATHLVGKWHLGfytweytptnrgfdsfygyyggaedyythtsgGANDYGNDDLRDNEEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 144 SVLQVGRNITriKLLVR---KFLQTQD-DRPFFLYVAFHDPHrcghsqpqygtfcekFGNGEsgmgripdwtPQAYDPLD 219
Cdd:cd16029 155 AWDYNGTYST--DLFTDravDIIENHDpSKPLFLYLAFQAVH---------------APLQV----------PPEYADPY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 220 VLVPYFVPNTpaARADLAAqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRT--N---------LYWP 288
Cdd:cd16029 208 EDKFAHIKDE--DRRTYAA---MVSALDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsNyplrggkntLWEG 282
|
330 340
....*....|....*....|....*
gi 1209857043 289 GTAEPLLVSSPEHPKRWGQVSEAYV 313
Cdd:cd16029 283 GVRVPAFVWSPLLPPKRGTVSDGLM 307
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
22-316 |
8.89e-28 |
|
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: 113.33 E-value: 8.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNS 100
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSRETPNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNA--HARNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 101 F----------DKVRSLPLLLSQAGVRTGIIGKKHVGPETVY-P----FDFAYTEENGSV-----------------LQV 148
Cdd:cd16157 79 YtpqnivggipDSEILLPELLKKAGYRNKIVGKWHLGHRPQYhPlkhgFDEWFGAPNCHFgpydnkaypnipvyrdwEMI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 149 GR--------------NITRIkLLVR--KFLQTQ--DDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGnGESGMGRIPDw 210
Cdd:cd16157 159 GRyyeefkidkktgesNLTQI-YLQEalEFIEKQhdAQKPFFLYWAPDATH-----APVYAS--KPFL-GTSQRGLYGD- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 211 tpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI-------------P 277
Cdd:cd16157 229 -------------------------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAalisapeqggsngP 277
|
330 340 350
....*....|....*....|....*....|....*....
gi 1209857043 278 FPSGRTNLYWPGTAEPLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16157 278 FLCGKQTTFEGGMREPAIAWWPGHIKP-GQVSHQLGSLM 315
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
22-316 |
1.81e-27 |
|
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: 111.90 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 22 PRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQdvHHFNSF 101
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYGGHPAKTPNIDRLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNS--YFRKVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 102 DKVRSLPLLLSQAGVRTGIIGK---KHVGPE-------TVYPFDFAYTEENGSVLQVGRNITR----------------- 154
Cdd:cd16030 80 PDAVTLPQYFKENGYTTAGVGKifhPGIPDGdddpaswDEPPNPPGPEKYPPGKLCPGKKGGKgggggpaweaadvpdea 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 155 ----------IKLLVRKFlqtQDDRPFFLYVAFHDPHRcghsqP---------QYGTFCEKFGNGESGMG----RIPDWT 211
Cdd:cd16030 160 ypdgkvadeaIEQLRKLK---DSDKPFFLAVGFYKPHL-----PfvapkkyfdLYPLESIPLPNPFDPIDlpevAWNDLD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 212 --PQAYDPLDVLVPYFVPNTPAARADLAAQ--YTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGipFPSG------ 281
Cdd:cd16030 232 dlPKYGDIPALNPGDPKGPLPDEQARELRQayYASVSYVDAQVGRVLDALEELGLADNTIVVLWSDHG--WHLGehghwg 309
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1209857043 282 -RTNlyWpgtaE-----PLLVSSPEHPKRwGQVSEAYVSLL 316
Cdd:cd16030 310 kHTL--F----EeatrvPLIIRAPGVTKP-GKVTDALVELV 343
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
21-275 |
3.32e-27 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 111.68 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGFES-GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlHQDVhhfN 99
Cdd:PRK13759 6 KP-NIILIMVDQMRGDClGCNGNKAVETPNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVG-YGDV---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKVRSLPLLLSQAGVRTGIIGKKHVGPETV--------------------YPFDFAYTEENGSVLQ---VGRNITRIK 156
Cdd:PRK13759 81 PWNYKNTLPQEFRDAGYYTQCIGKMHVFPQRNllgfhnvllhdgylhsgrneDKSQFDFVSDYLAWLRekaPGKDPDLTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 157 LLVR--------------------------KFLQTQD-DRPFFLYVAFHDPHRcGHSQPQYgtFCEKFGNGESGMGRIPD 209
Cdd:PRK13759 161 IGWDcnswvarpwdleerlhptnwvgsesiEFLRRRDpTKPFFLKMSFARPHS-PYDPPKR--YFDMYKDADIPDPHIGD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209857043 210 WT------PQAYDPlDVLVPYFvPNTPAARAdLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:PRK13759 238 WEyaedqdPEGGSI-DALRGNL-GEEYARRA-RAAYYGLITHIDHQIGRFLQALKEFGLLDNTIILFVSDHG 306
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
24-316 |
2.09e-26 |
|
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: 107.28 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADD-GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYG----LHQDV--- 95
Cdd:cd16032 2 NILLIMADQlTAAALPAYGNTVVKTPNLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAYDnaaeFPADIptf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 96 -HHfnsfdkvrslpllLSQAGVRTGIIGKKH-VGPETVYPFDfaYTEEngsvlqVGRNITRiKL--LVRKflqtQDDRPF 171
Cdd:cd16032 82 aHY-------------LRAAGYRTALSGKMHfVGPDQLHGFD--YDEE------VAFKAVQ-KLydLARG----EDGRPF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 172 FLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwtpqayDPLDVLVPYFVPNTPAARadlAAQYTTVGRMDQGVG 251
Cdd:cd16032 136 FLTVSFTHPH----------------------------------DPYVIPQEYWDLYVRRAR---RAYYGMVSYVDDKVG 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209857043 252 LVLQELRDAGVLNDTLVIFTSDN-------GIPFpsgRTNLYWPGTAEPLLVSSPE--HPKRwgqVSEAyVSLL 316
Cdd:cd16032 179 QLLDTLERTGLADDTIVIFTSDHgdmlgerGLWY---KMSFFEGSARVPLIISAPGrfAPRR---VAEP-VSLV 245
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
24-275 |
2.23e-26 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293761 [Multi-domain] Cd Length: 372 Bit Score: 108.00 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGF-ESGAYNNSAI---ATPHLDALARRSLLFRNaFTSVSSCSPSRASLLTG---------LPQHQNGMYG 90
Cdd:cd16142 2 NILVILGDDIGWgDLGCYGGGIGrgaPTPNIDRLAKEGLRFTS-FYVEPSCTPGRAAFITGrhpirtgltTVGLPGSPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 91 LHqdvhhfnsfDKVRSLPLLLSQAGVRTGIIGKKHVG--PE---TVYPFD----FAYT---EEngsvlQVGRNITRIKll 158
Cdd:cd16142 81 LP---------PWEPTLAELLKDAGYATAQFGKWHLGdeDGrlpTDHGFDefygNLYHtidEE-----IVDKAIDFIK-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 159 vRkflQTQDDRPFFLYVAFHDPHRCGHSQPQYgtfcekfgngesgMGRIPDWTPQAydplDVLVpyfvpntpaaradlaa 238
Cdd:cd16142 145 -R---NAKADKPFFLYVNFTKMHFPTLPSPEF-------------EGKSSGKGKYA----DSMV---------------- 187
|
250 260 270
....*....|....*....|....*....|....*..
gi 1209857043 239 qyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16142 188 ------ELDDHVGQILDALDELGIADNTIVIFTTDNG 218
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
22-275 |
5.20e-25 |
|
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: 105.60 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 22 PRNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhQDVHHFNS 100
Cdd:cd16158 1 PPNIVLLFADDLGYgDLGCYGHPSSSTPNLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYQVRSGVY---PGVFYPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 101 FDkvrSLPL-------LLSQAGVRTGIIGKKH--VGPETVY-P----FDF----AYTEENG------------------- 143
Cdd:cd16158 78 RG---GLPLnettiaeVLKTVGYQTAMVGKWHlgVGLNGTYlPthqgFDHylgiPYSHDQGpcqnltcfppnipcfggcd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 144 ------------SVLQVGRNITRIKLLVRKFLQ------TQDDRPFFLYVAFHDPHrcghsQPQYGTfcEKFGNgESGMG 205
Cdd:cd16158 155 qgevpcplfyneSIVQQPVDLLTLEERYAKFAKdfiadnAKEGKPFFLYYASHHTH-----YPQFAG--QKFAG-RSSRG 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 206 RIPDwtpqaydpldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16158 227 PFGD--------------------------------ALAELDGSVGELLQTLKENGIDNNTLVFFTSDNG 264
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
22-316 |
1.54e-24 |
|
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze sulfate esters in a wide variety of substrates such as glycosaminoglycans, steroid sulfates, or sulfolipids. ARSG has arylsulfatase activity toward different pseudosubstrates like p-nitrocatechol sulfate and 4-methylumbelliferyl sulfate. An active site Cys is post-translationally converted to the critical active site C(alpha)-formylglycine. ARSG mRNA expression was found to be tissue-specific with highest expression in liver, kidney, and pancreas, suggesting a metabolic role of ARSG that might be associated with a non-classified lysosomal storage disorder.
Pssm-ID: 293780 [Multi-domain] Cd Length: 383 Bit Score: 102.93 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 22 PRNALLLLADDGGFESGAYNN--SAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHFN 99
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWapNAILTPNLDKLAAEGTRFVDWYSAASVCSPSRASLMT-------GRLGLRNGVGHNF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKVRSLPL-------LLSQAGVRTGIIGKKHVGPETVY-P----FDFAY--TEENGSVLQvgrniTRIKLLVRKFLQ- 164
Cdd:cd16161 74 LPTSVGGLPLnettlaeVLRQAGYATGMIGKWHLGQREAYlPnsrgFDYYFgiPFSHDSSLA-----DRYAQFATDFIQr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 165 -TQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPQAYDPLdvlvpyfVPNTPAARADLAAqytTV 243
Cdd:cd16161 149 aSAKDRPFFLYAALAHVH-----------------------------VPLANLPR-------FQSPTSGRGPYGD---AL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 244 GRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG--------IPFPSG---RTNLYWP---------GTAEPLLVSSPEHPK 303
Cdd:cd16161 190 QEMDDLVGQIMDAVKHAGLKDNTLTWFTSDNGpwevkcelAVGPGTgdwQGNLGGSvakastwegGHREPAIVYWPGRIP 269
|
330
....*....|...
gi 1209857043 304 RwGQVSEAYVSLL 316
Cdd:cd16161 270 A-NSTSAALVSTL 281
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
38-316 |
6.46e-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: 293771 [Multi-domain] Cd Length: 373 Bit Score: 101.15 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY----GLHQDvhhfnsfdkVRSLPLLLSQ 113
Cdd:cd16152 18 GCYGQPLDLTPNLDALAEEGVLFENAFTPQPVCGPARACLQTGLYPTETGCFrngiPLPAD---------EKTLAHYFRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 114 AGVRTGIIGKKHVGpetVYPFDFayteengsvlqvgrnITRIKLlvrKFLQT-QDDRPFFLYVAFHDPHrcgHsQPQYGT 192
Cdd:cd16152 89 AGYETGYVGKWHLA---GYRVDA---------------LTDFAI---DYLDNrQKDKPFFLFLSYLEPH---H-QNDRDR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 193 F------CEKFGNGesgmgripdWTPQAYDPLdvlvpyfvPNTpaARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDT 266
Cdd:cd16152 144 YvapegsAERFANF---------WVPPDLAAL--------PGD--WAEELPDYLGCCERLDENVGRIRDALKELGLYDNT 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1209857043 267 LVIFTSDNGIPFPSgRTNLYWPGTAE-----PLLVSSPehPKRWGQVSEAYVSLL 316
Cdd:cd16152 205 IIVFTSDHGCHFRT-RNAEYKRSCHEssirvPLVIYGP--GFNGGGRVEELVSLI 256
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-275 |
1.36e-22 |
|
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: 95.91 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFESGAYNNSAIA-----------TPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGL- 91
Cdd:cd16153 3 NILWIITDDQRVDSLSCYNNAHTgksesrlgyveSPNIDALAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYGFe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 92 --HQDVHHFNsfdkvRSLPLLLSQAGVRTGIIGKKHVGPETVYpfdfayteengsvlqVGRNITRIKLLVRKFLQTQD-D 168
Cdd:cd16153 83 aaHPALDHGL-----PTFPEVLKKAGYQTASFGKSHLEAFQRY---------------LKNANQSYKSFWGKIAKGADsD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 169 RPFFLYVAFHDPHrcghsqpqygtfcekfgngesgmgripdwTPqaydpldVLVpyfvpntPAARADLAAQYTTVGRMDQ 248
Cdd:cd16153 143 KPFFVRLSFLQPH-----------------------------TP-------VLP-------PKEFRDRFDYYAFCAYGDA 179
|
250 260 270
....*....|....*....|....*....|
gi 1209857043 249 GVGLVLQELRDAGVLND---TLVIFTSDNG 275
Cdd:cd16153 180 QVGRAVEAFKAYSLKQDrdyTIVYVTGDHG 209
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
23-275 |
4.90e-22 |
|
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: 96.56 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 23 RNALLLLADDGGFE-SGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMY--GLHQDVHHfn 99
Cdd:cd16028 1 RNVLFITADQWRADcLSCLGHPLVKTPNLDRLAAEGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVwnGTPLDARH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 sfdkvRSLPLLLSQAGVRTGIIGKKHVGP----------------------ETVYPFDFaYTEENGSVlqvgRNITRiKL 157
Cdd:cd16028 79 -----LTLALELRKAGYDPALFGYTDTSPdprglapldprllsyelampgfDPVDRLDE-YPAEDSDT----AFLTD-RA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 158 LvrKFLQTQDDRPFFLYVAFHDPH----------------------RCGHSQ------PQYGTFCEKFGNGESGMGRIPD 209
Cdd:cd16028 148 I--EYLDERQDEPWFLHLSYIRPHppfvapapyhalydpadvpppiRAESLAaeaaqhPLLAAFLERIESLSFSPGAANA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1209857043 210 WTPqaydpldvlvpyfvpnTPAARADLAAQYT-TVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16028 226 ADL----------------DDEEVAQMRATYLgLIAEVDDHLGRLFDYLKETGQWDDTLIVFTSDHG 276
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
24-316 |
4.71e-21 |
|
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its homologous proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293779 [Multi-domain] Cd Length: 445 Bit Score: 93.65 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFD 102
Cdd:cd16160 3 NIVLFFADDMGYgDLASYGHPTQERGPIDDMAAEGIRFTQAYSADSVCTPSRAALLTGRLPIRSGMYGGTRVFLPWDIGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 103 KVRS---LPLLLSQAGVRTGIIGKKHVG------------PE--------TVYPFDFAY----TEE-------NGSVLQV 148
Cdd:cd16160 83 LPKTevtMAEALKEAGYTTGMVGKWHLGinennhsdgahlPShhgfdfvgTNLPFTNSWacddTGRhvdfpdrSACFLYY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 149 GRNIT-----------RIKLLVRKFLQTQDDRPFFLYVAFhdphrcghSQPQYGTFCEKFGNGESGMGRIPDwtpqaydp 217
Cdd:cd16160 163 NDTIVeqpiqhehlteTLVGDAKSFIEDNQENPFFLYFSF--------PQTHTPLFASKRFKGKSKRGRYGD-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 218 ldvlvpyfvpntpaaradlaaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI------------PFPSGRTN- 284
Cdd:cd16160 227 ------------------------NINEMSWAVGEVLDTLVDTGLDQNTLVFFLSDHGPhveycleggstgGLKGGKGNs 282
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1209857043 285 ----------LYWPGTAEPllvsspehpkrwgQVSEAYVSLL 316
Cdd:cd16160 283 weggirvpfiAYWPGTIKP-------------RVSHEVVSTM 311
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
24-297 |
2.86e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 87.79 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLADDGGFESGA---YNNSAIATPHLDALARRSLLFRNAFtSVSSCSPSRASLLTglpqhqnGMYGLHQDVHHF-- 98
Cdd:cd16154 2 NILLIIADDQGLDSSAqysLSSDLPVTPTLDSLANSGIVFDNLW-ATPACSPTRATILT-------GKYGFRTGVLAVpd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 99 NSFDKVRSLPLLL----SQAGVRTGIIGKKHVG------PETVYPFDFA---------YTE----ENGSVLQVGR-NITR 154
Cdd:cd16154 74 ELLLSEETLLQLLikdaTTAGYSSAVIGKWHLGgndnspNNPGGIPYYAgilgggvqdYYNwnltNNGQTTNSTEyATTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 155 IKLLVRKFLQTQdDRPFFLYVAFHDPHRCGHSQPqygtfcekfgNGESGMGRIPDWTPQAYDPLdvlvPYFvpntpaara 234
Cdd:cd16154 154 LTNLAIDWIDQQ-TKPWFLWLAYNAPHTPFHLPP----------AELHSRSLLGDSADIEANPR----PYY--------- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209857043 235 dLAAqyttVGRMDQGVGLVLQELrDAGVLNDTLVIFTSDNGIP-------FPSGRT--NLYWPGTAEPLLVS 297
Cdd:cd16154 210 -LAA----IEAMDTEIGRLLASI-DEEERENTIIIFIGDNGTPgqvvdlpYTRNHAkgSLYEGGINVPLIVS 275
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
48-275 |
8.28e-19 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293759 [Multi-domain] Cd Length: 311 Bit Score: 85.72 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 48 PHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYglhqDVHHFNSF----DKVRSLPLLLSQAGVRTGIIGK 123
Cdd:cd16035 27 PARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT----DTLGSPMQpllsPDVPTLGHMLRAAGYYTAYKGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 124 KHV--GPETVYPFDFAYTEEngsvlqvgrnitRIKLLVRKFLQTQDDRPFFLYVAFHDPHrcghsqpqygtfcekfgnge 201
Cdd:cd16035 103 WHLsgAAGGGYKRDPGIAAQ------------AVEWLRERGAKNADGKPWFLVVSLVNPH-------------------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1209857043 202 sgmgripdwtpqaydplDVLvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16035 151 -----------------DIM--FPPDDEERWRRFRNFYYNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHG 205
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
38-309 |
1.21e-18 |
|
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: 86.67 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGlhqdvhhfNSF---DKVRSLPLLLSQA 114
Cdd:cd16156 17 GCYGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWT--------NCMalgDNVKTIGQRLSDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 115 GVRTGIIGKKHV-------------GPETVYPFDFA-YTEE----------NGSVLQVGRNIT-------RIKLLVRKFL 163
Cdd:cd16156 89 GIHTAYIGKWHLdggdyfgngicpqGWDPDYWYDMRnYLDElteeerrksrRGLTSLEAEGIKeeftyghRCTNRALDFI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 164 QTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFgngesgmgRIPDwTPQAYDPLDvlvpyfvpNTPA-ARADLAAQYTT 242
Cdd:cd16156 169 EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDF--------EFPK-GENAYDDLE--------NKPLhQRLWAGAKPHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 243 VGR---------------MDQGVGLVLQELRDagVLNDTLVIFTSDNGIPFpsGRTNLYWPGTAE-------PLLVSSPE 300
Cdd:cd16156 232 DGDkgtikhplyfgcnsfVDYEIGRVLDAADE--IAEDAWVIYTSDHGDML--GAHKLWAKGPAVydeitniPLIIRGKG 307
|
....*....
gi 1209857043 301 HPKRWGQVS 309
Cdd:cd16156 308 GEKAGTVTD 316
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
23-314 |
3.05e-16 |
|
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: 77.08 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 23 RNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFR-NAFTSVSSCSPSRASLLTGLPQHQNGMYG--------LH 92
Cdd:cd00016 1 KHVVLIVLDGLGAdDLGKAGNPAPTTPNLKRLASEGATFNfRSVSPPTSSAPNHAALLTGAYPTLHGYTGngsadpelPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 93 QDVHHFNSFDkvrSLPLLLSQAGVRTGIIGkkhvgpetvypfdfayteengsvlqvgrnitrikllVRKFL-QTQDDRPF 171
Cdd:cd00016 81 RAAGKDEDGP---TIPELLKQAGYRTGVIG------------------------------------LLKAIdETSKEKPF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 172 FLYVAFHDPHRCGHSqpqygtfcekfgngesgmgriPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVG 251
Cdd:cd00016 122 VLFLHFDGPDGPGHA---------------------YGPNTPEY------------------------YDAVEEIDERIG 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1209857043 252 LVLQELRDAGVLNDTLVIFTSDNG-IPFPSGRT--NLYWPGTAE-----PLLVSSPEHPKrwGQVSEAYVS 314
Cdd:cd00016 157 KVLDALKKAGDADDTVIIVTADHGgIDKGHGGDpkADGKADKSHtgmrvPFIAYGPGVKK--GGVKHELIS 225
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
21-275 |
2.37e-14 |
|
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: 73.86 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 21 RPrNALLLLADDGGF-ESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMyGLHQDVHHFN 99
Cdd:cd16159 1 KP-NIVLFMADDLGIgDVGCFGNDTIRTPNIDRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYPIRSGM-ASSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 100 SFDKVRSLP-------LLLSQAGVRTGIIGKKHVG--PETV---------YPFDFAY-----------TEENGSVLQVGR 150
Cdd:cd16159 79 FTASSGGLPpnettfaEVLKQQGYSTALIGKWHLGlhCESRndfchhplnHGFDYFYglpltnlkdcgDGSNGEYDLSFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 151 N-----------------------------------------------ITRIK----LLVR------------------- 160
Cdd:cd16159 159 PlfplltafvlitaltiflllylgavskrffvfllilsllfislffllLITNRyfncILMRnhevveqpmslenltqrlt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 161 ----KFLQTQDDRPFFLYVAFHDPHRCGHSQPqygtfceKFgNGESGMGRIPDwtpqaydpldvlvpyfvpntpaaradl 236
Cdd:cd16159 239 keaiSFLERNKERPFLLVMSFLHVHTALFTSK-------KF-KGRSKHGRYGD--------------------------- 283
|
330 340 350
....*....|....*....|....*....|....*....
gi 1209857043 237 aaqytTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNG 275
Cdd:cd16159 284 -----NVEEMDWSVGQILDALDELGLKDNTFVYFTSDNG 317
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
10-276 |
4.88e-11 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 63.23 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 10 ALLLVLGLCRARPRNALLLLADdgGFesGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCS-PSRASLLTGLP--QHQ- 85
Cdd:COG1524 11 SLLAAAAAAAPPAKKVVLILVD--GL--RADLLERAHAPNLAALAARGVYARPLTSVFPSTTaPAHTTLLTGLYpgEHGi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 86 --NGMY-----------GLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIG-KKHVGPETV-YPFDFAYteeNGSVLQVGR 150
Cdd:COG1524 87 vgNGWYdpelgrvvnslSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVFwPSFEGSGLIdAARPYPY---DGRKPLLGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 151 NITRiKLLVRKFLQT-QDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNT 229
Cdd:COG1524 164 PAAD-RWIAAAALELlREGRPDLLLVYLPDLDYAGH---RYG-----------------------------------PDS 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1209857043 230 PAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:COG1524 205 PEYRAALR-------EVDAALGRLLDALKARGLYEGTLVIVTADHGM 244
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
26-276 |
2.30e-09 |
|
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: 57.59 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 26 LLLLADdgGFESgAYNNSAIATPHLDALARRSLLF---RNAFTSVSScsPSRASLLTGLP--QHQ---NGMY-------G 90
Cdd:cd16018 4 IVISID--GFRW-DYLDRAGLTPNLKRLAEEGVRAkyvKPVFPTLTF--PNHYSIVTGLYpeSHGivgNYFYdpktneeF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 91 LHQDVHHFNSFDKVRSLPLLLSQAGVRTGII------GKKHVGPETVYPFDFAYTEENGSVLqvgrNITRIKLLVRKFlq 164
Cdd:cd16018 79 SDSDWVWDPWWIGGEPIWVTAEKAGLKTASYfwpgseVAIIGYNPTPIPLGGYWQPYNDSFP----FEERVDTILEWL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 165 tQDDRPFFLYVAFHDPHRCGHsqpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvg 244
Cdd:cd16018 153 -DLERPDLILLYFEEPDSAGH---KYG-----------------------------------PDSPEVNEALK------- 186
|
250 260 270
....*....|....*....|....*....|..
gi 1209857043 245 RMDQGVGLVLQELRDAGVLNDTLVIFTSDNGI 276
Cdd:cd16018 187 RVDRRLGYLIEALKERGLLDDTNIIVVSDHGM 218
|
|
| Phosphodiest |
pfam01663 |
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ... |
47-276 |
4.59e-09 |
|
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: 57.05 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 47 TPHLDALARRSLLFRNAFTSV-SSCSPSRASLLTGLPQHQNGMYG-----------LHQDVHHFNSFDKVRSLPLL--LS 112
Cdd:pfam01663 20 TPNLAALAKEGVSAPNLTPVFpTLTFPNHYTLVTGLYPGSHGIVGntfydpktgeyLVFVISDPEDPRWWQGEPIWdtAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 113 QAGVRTGII----GKKHVGPETVYPFDFAYTEENGSVLQVGR--NITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHs 186
Cdd:pfam01663 100 KAGVRAAALfwpgSEVDYSTYYGTPPRYLKDDYNNSVPFEDRvdTAVLQTWLDLPFADVAAERPDLLLVYLEEPDYAGH- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 187 qpQYGtfcekfgngesgmgripdwtpqaydpldvlvpyfvPNTPAARADLAaqyttvgRMDQGVGLVLQELRDAGVLNDT 266
Cdd:pfam01663 179 --RYG-----------------------------------PDSPEVEDALR-------RVDRAIGDLLEALDERGLFEDT 214
|
250
....*....|
gi 1209857043 267 LVIFTSDNGI 276
Cdd:pfam01663 215 NVIVVSDHGM 224
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
33-314 |
9.65e-09 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 56.97 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 33 GGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLP-QHQNGMYGLHQDVHHFnsfdkvrSLPLLL 111
Cdd:COG1368 246 SDFFIGALGNGKDVTPFLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPpLPGGSPYKRPGQNNFP-------SLPSIL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 112 SQAGVRTGIIgkkHVGPET------VYP---FDFAYTEENgsvLQVGRNIT-RI--KLLVRKFLQT--QDDRPFFLYV-- 175
Cdd:COG1368 319 KKQGYETSFF---HGGDGSfwnrdsFYKnlgFDEFYDRED---FDDPFDGGwGVsdEDLFDKALEEleKLKKPFFAFLit 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 176 -AFHDPhrcghsqpqYgtfceKFGNGESGMGRIPDWTPQAYdpldvlvpyfvpntpaaradlaaqYTTVGRMDQGVGLVL 254
Cdd:COG1368 393 lSNHGP---------Y-----TLPEEDKKIPDYGKTTLNNY------------------------LNAVRYADQALGEFI 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209857043 255 QELRDAGVLNDTLVIFTSDNGIPFPsGRTNLYWPGTAE--PLLVSSPEHPKrwGQVSEAYVS 314
Cdd:COG1368 435 EKLKKSGWYDNTIFVIYGDHGPRSP-GKTDYENPLERYrvPLLIYSPGLKK--PKVIDTVGS 493
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
24-339 |
2.65e-08 |
|
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: 54.85 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 24 NALLLLAD--DGGFeSGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHqngmygLHQDVHHFNSF 101
Cdd:cd16171 2 NVVMVMSDsfDGRL-TFRPGNQVVDLPYINFMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTH------LTESWNNYKGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 102 DK-VRSLPLLLSQAGVRTGIIGKKHV--GPETVYPFDFAYTEENGSVL-QVGR---NITRIKLLVRKFL---QTQD---- 167
Cdd:cd16171 75 DPnYPTWMDRLEKHGYHTQKYGKLDYtsGHHSVSNRVEAWTRDVPFLLrQEGRptvNLVGDRSTVRVMLkdwQNTDkavh 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 168 ---------DRPFFLYVAFHDPHrcghsqpQYGTfcekfgngesgmgripdwtpqaydpldvlvPYFVPNTPAARADLAA 238
Cdd:cd16171 155 wirkeapnlTQPFALYLGLNLPH-------PYPS------------------------------PSMGENFGSIRNIRAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 239 QYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGR----TNLYWPGTAEPLLVSSPEHPKrwGQVSEAYVS 314
Cdd:cd16171 198 YYAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHGELAMEHRqfykMSMYEGSSHVPLLIMGPGIKA--GQQVSDVVS 275
|
330 340
....*....|....*....|....*....
gi 1209857043 315 LLGTEAQRDDVA----VRGVGSTRHLPLL 339
Cdd:cd16171 276 LVDIYPTMLDIAgvpqPQNLSGYSLLPLL 304
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
38-280 |
3.73e-07 |
|
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: 51.14 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 38 GAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRA--SLLTGLPQHQNGMYGLHQDVHHfnsfdKVRSLPLLLSQAG 115
Cdd:cd16015 17 DKDVGGEDLTPNLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLPPLPLGSGSYTLYKLN-----PLPSLPSILKEQG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 116 VRTGIIgkkHVGP------ETVYP---FDFAYTEENGSVLQVGRNITRI--KLLVRKF---LQTQDDRPFFLYV---AFH 178
Cdd:cd16015 92 YETIFI---HGGDasfynrDSVYPnlgFDEFYDLEDFPDDEKETNGWGVsdESLFDQAleeLEELKKKPFFIFLvtmSNH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209857043 179 DPhrcghsqpqYGTFCEKFgngesgmgripdwtpqaydpldvlvpYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELR 258
Cdd:cd16015 169 GP---------YDLPEEKK--------------------------DEPLKVEEDKTELENYLNAIHYTDKALGEFIEKLK 213
|
250 260
....*....|....*....|..
gi 1209857043 259 DAGVLNDTLVIFTSDNGIPFPS 280
Cdd:cd16015 214 KSGLYENTIIVIYGDHLPSLGS 235
|
|
| |
