|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
53-408 |
0e+00 |
|
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: 539.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDVELGSLNFMPRTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTN--NDNCSSPQWQA 130
Cdd:cd16147 1 RPNIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNspPGGGYPKFWQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 131 THETRSYATYLSNAGYRTGYFGKYLNKY----NGSYIPPGWREWGGLIMNSKYYNYSINlNGQKIKHGFDYAKDYYPDLI 206
Cdd:cd16147 81 GLERSTLPVWLQEAGYRTAYAGKYLNGYgvpgGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 207 ANDSIAFLRSSKQQNqrKPVLLTMSFPAPHGPEDSAPQYSHLFFNVT-THHTPSYDHAPNPDKQWILRVTEPMQPvHKRF 285
Cdd:cd16147 160 ANKALDFLRRAAADD--KPFFLVVAPPAPHGPFTPAPRYANLFPNVTaPPRPPPNNPDVSDKPHWLRRLPPLNPT-QIAY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 286 TNLLMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFDVRVPFLIRGPGIQASKV 365
Cdd:cd16147 237 IDELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVT 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 442619385 366 VNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVR 408
Cdd:cd16147 317 VDQLVSNIDLAPTILDLAGAPPPSDMDGRSCGDSNNNTYKCVR 359
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
52-418 |
3.74e-96 |
|
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: 312.54 E-value: 3.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 52 RRPNIILILTDDQdvELGSLNFMPRTL-------RLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCS 124
Cdd:cd16031 1 KRPNIIFILTDDH--RYDALGCYGNPIvktpnidRLAKEG-VRFDNAFVTTSICAPSRASILTGQYSHRHGVTDNNGPLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 125 SPqWQathetRSYATYLSNAGYRTGYFGKYLNKYNGSYIPPGWREWGGLIMNSKYYNYSINLNGQKIKHgfdyaKDYYPD 204
Cdd:cd16031 78 DA-SQ-----PTYPKLLRKAGYQTAFIGKWHLGSGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVGQ-----KGYVTD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 LIANDSIAFLRSSKQQnqrKPVLLTMSFPAPHGPEDSAPQYSHLFFNVT-----THHTPSYDHAPNPDKQWILRVTEPMQ 279
Cdd:cd16031 147 IITDKALDFLKERDKD---KPFCLSLSFKAPHRPFTPAPRHRGLYEDVTipepeTFDDDDYAGRPEWAREQRNRIRGVLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 280 -PVHKRFTNLLMTKR-LQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIkGKSFPFEFDVRVPFLIRG 357
Cdd:cd16031 224 gRFDTPEKYQRYMKDyLRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGLF-DKRLMYEESIRVPLIIRD 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619385 358 PG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLlsRNRAVRDnWPDSFLIE 418
Cdd:cd16031 303 PRlIKAGTVVDALVLNIDFAPTILDLAGVPIPEDMQGRSLLPLL--EGEKPVD-WRKEFYYE 361
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
42-409 |
3.95e-78 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 262.12 E-value: 3.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 42 FSRDSNSARERRPNIILILTDDQDV-ELGSLNF----MPrTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMV 116
Cdd:COG3119 12 LAAAAAAAAAKRPNILFILADDLGYgDLGCYGNplikTP-NIDRLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 117 FTNNDNCSSPqwqATHETRSYATYLSNAGYRTGYFGKYLNkyngsyippgwrewgglimnskyynysinlngqkikhgfd 196
Cdd:COG3119 91 TDNGEGYNGG---LPPDEPTLAELLKEAGYRTALFGKWHL---------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 197 yakdYYPDLIANDSIAFLRssKQQNQRKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHHTPSYDHAPNPDKQWilrvte 276
Cdd:COG3119 128 ----YLTDLLTDKAIDFLE--RQADKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPLPPNLAPRDLTEEEL------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 277 pmqpvhkrftNLLMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFDVRVPFLIR 356
Cdd:COG3119 196 ----------RRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVR 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442619385 357 GPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:COG3119 266 WPGkIKAGSVSDALVSLIDLLPTLLDLAGVPIPEDLDGRSLLPLLTGEKAEWRD 319
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
54-395 |
4.45e-60 |
|
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: 205.75 E-value: 4.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ--DVeLGSLNF----MPrTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNcssPQ 127
Cdd:cd16022 1 PNILLIMTDDLgyDD-LGCYGNpdikTP-NLDRLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGNVGN---GG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 128 WQATHETrSYATYLSNAGYRTGYFGKylnkyngsyippgwreWgglimnskyynysinlngqkikHgfdyakdyypdlia 207
Cdd:cd16022 76 GLPPDEP-TLAELLKEAGYRTALIGK----------------W----------------------H-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 208 NDSIAFLRsskQQNQRKPVLLTMSFPAPHGPedsapqyshlffnvtthhtpsydhapnpdkqwilrvtepmqpvhkrFTN 287
Cdd:cd16022 103 DEAIDFIE---RRDKDKPFFLYVSFNAPHPP----------------------------------------------FAY 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 288 LLMTKRlqtlqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFDVRVPFLIRGPG-IQASKVV 366
Cdd:cd16022 134 YAMVSA------IDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIPAGQVS 207
|
330 340
....*....|....*....|....*....
gi 442619385 367 NEIVLNVDLAPTFLDMGGVPTPQHMDGRS 395
Cdd:cd16022 208 DALVSLLDLLPTLLDLAGIEPPEGLDGRS 236
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
54-409 |
2.10e-56 |
|
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: 200.04 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVELGSLNF----MPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNH-MvfTNNDncsSPQW 128
Cdd:cd16027 1 PNILWIIADDLSPDLGGYGGnvvkTPNLDRLAAEG-VRFTNAFTTAPVCSPSRSALLTGLYPHQNgA--HGLR---SRGF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 129 QATHETRSYATYLSNAGYRTGYFGKYlnKYNGSYIPPGWrewgglimnskYYNYSINLNGQKIKHGFDYAKDyypdlian 208
Cdd:cd16027 75 PLPDGVKTLPELLREAGYYTGLIGKT--HYNPDAVFPFD-----------DEMRGPDDGGRNAWDYASNAAD-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 209 dsiaFLRSSKQQnqrKPVLLTMSFPAPHGPEDSAPQYshlffnvTTHHTPSYDHAPN--PDkqwilrvTEPMqpvhkRFT 286
Cdd:cd16027 134 ----FLNRAKKG---QPFFLWFGFHDPHRPYPPGDGE-------EPGYDPEKVKVPPylPD-------TPEV-----RED 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 287 nllMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYhlgqfGLIKGKSFPFEFDVRVPFLIRGPG-IQASKV 365
Cdd:cd16027 188 ---LADYYDEIERLDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPGkIKPGSV 259
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 442619385 366 VNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16027 260 SDALVSFIDLAPTLLDLAGIEPPEYLQGRSFLPLLKGEKDPGRD 303
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-428 |
2.48e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 201.30 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ--DVELGSLNFMPRT--LRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTN--NDNCSSPQ 127
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTpnIDRLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNveNAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 128 WQATHETrsYATYLSNAGYRTGYFGKYlnkYNGSYIPP---GWREWGGLimnskyynysinlngqkikhgfDYAKDYYpd 204
Cdd:cd16033 81 LPPGVET--FSEDLREAGYRNGYVGKW---HVGPEETPldyGFDEYLPV----------------------ETTIEYF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 lIANDSIAFLRSSKQQNqrKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHHTPSYDHAPNpDKQWILRVTEpmqpvhKR 284
Cdd:cd16033 132 -LADRAIEMLEELAADD--KPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFE-DKPYIYRRER------KR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 285 FTNLLMTKRLQ-----------TLqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFDVRVPF 353
Cdd:cd16033 202 WGVDTEDEEDWkeiiahywgyiTL--IDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRLWDKGPFMYEETYRIPL 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619385 354 LIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLlsRNRAVrDNWPDSFLIESSGRRETAEQ 428
Cdd:cd16033 280 IIKWPGvIAAGQVVDEFVSLLDLAPTILDLAGVDVPPKVDGRSLLPLL--RGEQP-EDWRDEVVTEYNGHEFYLPQ 352
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
53-421 |
1.17e-55 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293758 [Multi-domain] Cd Length: 399 Bit Score: 198.95 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTD-----------DQDVELGSLNfmprtlRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNND 121
Cdd:cd16034 1 KPNILFIFADqhraqalgcagDDPVKTPNLD------RLAKEG-VVFTNAVSNYPVCSPYRASLLTGQYPLTNGVFGNDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 122 NCSspqwqatHETRSYATYLSNAGYRTGYFGK--------YLNKYNGSYIPP----GWREWGGLIMNSKYYN--YSINlN 187
Cdd:cd16034 74 PLP-------PDAPTIADVLKDAGYRTGYIGKwhldgperNDGRADDYTPPPerrhGFDYWKGYECNHDHNNphYYDD-D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 188 GQKIkhgfdYAKDYYPDLIANDSIAFLRssKQQNQRKPVLLTMSFPAPHGPEDSAPQ-YSHLFfnvtthhtpsydhapnP 266
Cdd:cd16034 146 GKRI-----YIKGYSPDAETDLAIEYLE--NQADKDKPFALVLSWNPPHDPYTTAPEeYLDMY----------------D 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 267 DKQWILR--VTEPMQPVHkRFTNLL-----MTKrlqtlqSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIk 339
Cdd:cd16034 203 PKKLLLRpnVPEDKKEEA-GLREDLrgyyaMIT------ALDDNIGRLLDALKELGLLENTIVVFTSDHGDMLGSHGLM- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 340 GKSFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRDNWPDSFLIE 418
Cdd:cd16034 275 NKQVPYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPDTVEGRDLSPLLLGGKDDEPDSVLLQCFVP 354
|
...
gi 442619385 419 SSG 421
Cdd:cd16034 355 FGG 357
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
54-400 |
5.84e-51 |
|
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: 185.82 E-value: 5.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDD---QDVelgSLNFMP--RTLRL--LRDGGAEFRHAYTTTPMCCPARSSLLTGMY--------VHNHMVFT 118
Cdd:cd16144 1 PNIVLILVDDlgwADL---GCYGSKfyETPNIdrLAKEGMRFTQAYAAAPVCSPSRASILTGQYparlgitdVIPGRRGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 119 NNDNCSSPQWQATH---ETRSYATYLSNAGYRTGYFGKY-LNKYNGSYipP---------GWREWGGLIMNSKYYNYSIN 185
Cdd:cd16144 78 PDNTKLIPPPSTTRlplEEVTIAEALKDAGYATAHFGKWhLGGEGGYG--PedqgfdvniGGTGNGGPPSYYFPPGKPNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 186 LNGQkikhgfDYAKDYYPDLIANDSIAFLrsskQQNQRKPVLLTMSFPAPHGPedsapqyshlffnvttHHTPsydhapn 265
Cdd:cd16144 156 DLED------GPEGEYLTDRLTDEAIDFI----EQNKDKPFFLYLSHYAVHTP----------------IQAR------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 266 pdKQWILRVTEPMQPVHKRFTNLL---MtkrlqtLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLI---- 338
Cdd:cd16144 203 --PELIEKYEKKKKGLRKGQKNPVyaaM------IESLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGGPPtsna 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619385 339 ---KGKSFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTP--QHMDGRSILPLL 400
Cdd:cd16144 275 plrGGKGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPLPppQHLDGVSLVPLL 342
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
54-409 |
8.52e-50 |
|
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: 182.41 E-value: 8.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDqdveLG----SLNFM-----PRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDncS 124
Cdd:cd16145 1 PNIIFILADD----LGygdlGCYGQkkiktPNLDRLAAEG-MRFTQHYAGAPVCAPSRASLLTGLHTGHTRVRGNSE--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 125 SPQWQATHETRSYATYLSNAGYRTGYFGKYLNKYNGSYIPP---GWREWGG--------------LIMNSKYYNYSINLN 187
Cdd:cd16145 74 GGQDPLPPDDVTLAEVLKKAGYATAAFGKWGLGGPGTPGHPtkqGFDYFYGyldqvhahnyypeyLWRNGEKVPLPNNVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 188 GQKIKHGF--DYAKDYYPDLIANDSIAFLRsskqQNQRKPVLLTMSFPAPHGPedsapqyshlffnvttHHTPSYDHAPN 265
Cdd:cd16145 154 PPLDEGNNagGGGGTYSHDLFTDEALDFIR----ENKDKPFFLYLAYTLPHAP----------------LQVPDDGPYKY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 266 PDKQWILRVTEPMQPVHKRFTNllMTKRLqtlqsvDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSF-- 343
Cdd:cd16145 214 KPKDPGIYAYLPWPQPEKAYAA--MVTRL------DRDVGRILALLKELGIDENTLVVFTSDNGPHSEGGSEHDPDFFds 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442619385 344 --PF--------EFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16145 286 ngPLrgykrslyEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPEDIDGISLLPTLLGKPQQQQH 362
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
53-433 |
1.13e-48 |
|
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: 177.81 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQ--DVeLGS----LNFMPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDncSSP 126
Cdd:cd16152 1 KPNVIVFFTDQQrwDT-LGCygqpLDLTPNLDALAEEG-VLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGI--PLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 QwqathETRSYATYLSNAGYRTGYFGKY-LNKYNGSYIPpgwrewgglimnskyynysinlngqkikhgfDYAKDYYpdl 205
Cdd:cd16152 77 A-----DEKTLAHYFRDAGYETGYVGKWhLAGYRVDALT-------------------------------DFAIDYL--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 206 iandsiaflrssKQQNQRKPVLLTMSFPAPH---------GPEDSAPQYSHLFfnvtthhTPSyDHAPNP-DKQWILrvt 275
Cdd:cd16152 118 ------------DNRQKDKPFFLFLSYLEPHhqndrdryvAPEGSAERFANFW-------VPP-DLAALPgDWAEEL--- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 276 epmqPVHkrftnLLMTKRLqtlqsvDVAVERVYNELKELGELDNTYIVYTSDHGYHlgqFGLIKG--KSFPFEFDVRVPF 353
Cdd:cd16152 175 ----PDY-----LGCCERL------DENVGRIRDALKELGLYDNTIIVFTSDHGCH---FRTRNAeyKRSCHESSIRVPL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 354 LIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLlsrnRAVRDNWPDSFLIessgrretaeQIAESR 433
Cdd:cd16152 237 VIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVPEEMQGRSLLPLV----DGKVEDWRNEVFI----------QISESQ 302
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
54-385 |
7.74e-47 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 169.91 E-value: 7.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ-DVELGSLNFMPRT---LRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNndncssPQWQ 129
Cdd:pfam00884 1 PNVVLVLGESLrAPDLGLYGYPRPTtpfLDRLAEEGLLFSNFYSGGTLTAPSRFALLTGLPPHNFGSYVS------TPVG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 130 ATHETRSYATYLSNAGYRTGYFGKYLNKYNGSYIPP--GWREWGGLIMNSKYYNYsinlngQKIKHGFDYAKDYYPDLIA 207
Cdd:pfam00884 75 LPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCnlGFDKFFGRNTGSDLYAD------PPDVPYNCSGGGVSDEALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 208 NDSIAFLRSSKqqnqrKPVLLTMSFPAPHGPEDSAPQYshlffnvtthhtPSYDHAPNPDKQWILRVtepmqpvhkrftn 287
Cdd:pfam00884 149 DEALEFLDNND-----KPFFLVLHTLGSHGPPYYPDRY------------PEKYATFKPSSCSEEQL------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 288 llMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQ----FGLIKGKSFPfEFDVRVPFLIRGPG-IQA 362
Cdd:pfam00884 199 --LNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEgggyLHGGKYDNAP-EGGYRVPLLIWSPGgKAK 275
|
330 340
....*....|....*....|...
gi 442619385 363 SKVVNEIVLNVDLAPTFLDMGGV 385
Cdd:pfam00884 276 GQKSEALVSHVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-400 |
6.78e-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: 168.11 E-value: 6.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQdvelgSLNFMP-------RT--LRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCS 124
Cdd:cd16037 1 PNILIIMSDEH-----NPDAMGcyghpvvRTpnLDRLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNADPYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 125 SpqwqathETRSYATYLSNAGYRTGYFGKylnkyngsyippgwrewgglimnskyynysINLNGQKIKHGFDYAKDyypd 204
Cdd:cd16037 76 G-------DVPSWGHALRAAGYETVLIGK------------------------------LHFRGEDQRHGFRYDRD---- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 lIANDSIAFLRSSKQQNqrKPVLLTMSFPAPHGPedsapqyshlffnvtthhtpsYdHAPNPDKQWILR---------VT 275
Cdd:cd16037 115 -VTEAAVDWLREEAADD--KPWFLFVGFVAPHFP---------------------L-IAPQEFYDLYVRraraayyglVE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 276 EpmqpvhkrftnllmtkrlqtlqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIkGKSFPFEFDVRVPFLI 355
Cdd:cd16037 170 F-----------------------LDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGLW-GKSTMYEESVRVPMII 225
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 442619385 356 RGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLL 400
Cdd:cd16037 226 SGPGIPAGKRVKTPVSLVDLAPTILEAAGAPPPPDLDGRSLLPLA 270
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
53-409 |
1.38e-45 |
|
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: 170.45 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDVELGSL--NFMpRTLRL--LRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSSPQW 128
Cdd:cd16030 2 KPNVLFIAVDDLRPWLGCYggHPA-KTPNIdrLAARGVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNNSYFRKVAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 129 QAThetrSYATYLSNAGYRTGYFGKYLNKYNGSYI--PPGWREWGGLIMNSKYYNYSINLNGQKIKHG--------FDYA 198
Cdd:cd16030 81 DAV----TLPQYFKENGYTTAGVGKIFHPGIPDGDddPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpaweaADVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 199 KDYYPD-LIANDSIAFLRssKQQNQRKPVLLTMSFPAPHGPEdSAPQ-----YSHLFFNVTTHHTP---------SYDHA 263
Cdd:cd16030 157 DEAYPDgKVADEAIEQLR--KLKDSDKPFFLAVGFYKPHLPF-VAPKkyfdlYPLESIPLPNPFDPidlpevawnDLDDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 264 PNPDKQWILRVTEPMQPVHKRFTnllmtkrLQTLQS-------VDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFG 336
Cdd:cd16030 234 PKYGDIPALNPGDPKGPLPDEQA-------RELRQAyyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHLGEHG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442619385 337 LIkGKSFPFEFDVRVPFLIRGPGI-QASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16030 307 HW-GKHTLFEEATRVPLIIRAPGVtKPGKVTDALVELVDIYPTLAELAGLPAPPCLEGKSLVPLLKNPSAKWKD 379
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
54-426 |
8.44e-44 |
|
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: 164.65 E-value: 8.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVelGSLNFM-------PRTLRLLRDGgAEFRHAYTTtPMCCPARSSLLTGMYVHNHMVFtnndncssp 126
Cdd:cd16146 1 PNVILILTDDQGY--GDLGFHgnpilktPNLDRLAAES-VRFTNFHVS-PVCAPTRAALLTGRYPFRTGVW--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 qwqATHETRSY--------ATYLSNAGYRTGYFGKYLNKYNGSYIPP--GWREW----GGLI------MNSKYYNYSINL 186
Cdd:cd16146 68 ---HTILGRERmrldettlAEVFKDAGYRTGIFGKWHLGDNYPYRPQdrGFDEVlghgGGGIgqypdyWGNDYFDDTYYH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 187 NGQKIKHgfdyaKDYYPDLIANDSIAFLRsskqQNQRKPVLLTMSFPAPHGPedsapqyshlfFNVtthhtpsydhapnP 266
Cdd:cd16146 145 NGKFVKT-----EGYCTDVFFDEAIDFIE----ENKDKPFFAYLATNAPHGP-----------LQV-------------P 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 267 DKQWilrvtepmqpvhKRFTNLLMTKRLQTL----QSVDVAVERVYNELKELGELDNTYIVYTSDHGyhlGQFGLIKG-- 340
Cdd:cd16146 192 DKYL------------DPYKDMGLDDKLAAFygmiENIDDNVGRLLAKLKELGLEENTIVIFMSDNG---PAGGVPKRfn 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 341 ------KSFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQH--MDGRSILPLLLSRNravrDNW 411
Cdd:cd16146 257 agmrgkKGSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPEGikLDGRSLLPLLKGES----DPW 332
|
410
....*....|....*
gi 442619385 412 PDSFLIESSGRRETA 426
Cdd:cd16146 333 PERTLFTHSGRWPPP 347
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-409 |
6.02e-43 |
|
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: 159.30 E-value: 6.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ----DVELGSLNF-MPrTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFtnnDNCSSP-Q 127
Cdd:cd16035 1 PNILLILTDQEryppPWPAGWAALnLP-ARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVT---DTLGSPmQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 128 WQATHETRSYATYLSNAGYRTGYFGKY-LNKYNgsyippgwreWGGlimnskyynysinlngqkikhgfdYAKDyypDLI 206
Cdd:cd16035 77 PLLSPDVPTLGHMLRAAGYYTAYKGKWhLSGAA----------GGG------------------------YKRD---PGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 207 ANDSIAFLRSSKQQN-QRKPVLLTMSFPAPHgpeDSapqyshLFFnvtthhtpsydhaPNPDKQWIlrvtepmqpvhkRF 285
Cdd:cd16035 120 AAQAVEWLRERGAKNaDGKPWFLVVSLVNPH---DI------MFP-------------PDDEERWR------------RF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 286 TNLLmtkrLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLiKGKSF-PFEFDVRVPFLIRGPGI-QAS 363
Cdd:cd16035 166 RNFY----YNLIRDVDRQIGRVLDALDASGLADNTIVVFTSDHGEMGGAHGL-RGKGFnAYEEALHVPLIISHPDLfGTG 240
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442619385 364 KVVNEIVLNVDLAPTFLDMGGVPTPQHMD------GRSILPLLLS-RNRAVRD 409
Cdd:cd16035 241 QTTDALTSHIDLLPTLLGLAGVDAEARATeapplpGRDLSPLLTDaDADAVRD 293
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
52-409 |
1.34e-42 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 160.04 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 52 RRPNIILILTDDQdvelgslnfMPRTLRL-------------LRDGGAEFRHAY----TTTPMCCPARSSLLTGMYVHNh 114
Cdd:cd16155 1 KKPNILFILADDQ---------RADTIGAlgnpeiqtpnldrLARRGTSFTNAYnmggWSGAVCVPSRAMLMTGRTLFH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 115 mvFTNNDNCSSPQwqathETRSYATYLSNAGYRTGYFGKylnkyngsyippgwreWGglimnskyynysinlNGqkikhg 194
Cdd:cd16155 71 --APEGGKAAIPS-----DDKTWPETFKKAGYRTFATGK----------------WH---------------NG------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 195 fdyakdyypdlIANDSIAFLRssKQQNQRKPVLLTMSFPAPHGPEDSapqyshlffnvtthhTPSYDHAPNPDKqwiLRV 274
Cdd:cd16155 107 -----------FADAAIEFLE--EYKDGDKPFFMYVAFTAPHDPRQA---------------PPEYLDMYPPET---IPL 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 275 TEPMQPVHKrFTNLLMTKRLQTL---------------------QSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLG 333
Cdd:cd16155 156 PENFLPQHP-FDNGEGTVRDEQLapfprtpeavrqhlaeyyamiTHLDAQIGRILDALEASGELDNTIIVFTSDHGLAVG 234
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619385 334 QFGLIkGKSFPFEFDVRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16155 235 SHGLM-GKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIPESVEGKSLLPVIRGEKKAVRD 309
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-411 |
2.76e-41 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 156.22 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVE----LGSLNFmpRTLRL--LRDGGAEFRHAYTTtPMCCPARSSLLTGMY-VHNHMVFTNNDNcssp 126
Cdd:cd16151 1 PNIILIMADDLGYEcigcYGGESY--KTPNIdaLAAEGVRFNNAYAQ-PLCTPSRVQLMTGKYnFRNYVVFGYLDP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 qwqathETRSYATYLSNAGYRTGYFGKY-LNKYNGSYIPP---GWRE---WGGLIMNSKYYNYSINLNGQKIKHGFDYAK 199
Cdd:cd16151 74 ------KQKTFGHLLKDAGYATAIAGKWqLGGGRGDGDYPhefGFDEyclWQLTETGEKYSRPATPTFNIRNGKLLETTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 200 DYY-PDLIANDSIAFLRsskqQNQRKPVLLTMSFPAPHGPedsapqyshlfFNVTTHHTPSYDHAPNPDKQWilrvtepm 278
Cdd:cd16151 148 GDYgPDLFADFLIDFIE----RNKDQPFFAYYPMVLVHDP-----------FVPTPDSPDWDPDDKRKKDDP-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 279 qpvhKRFTNLLmtkrlqtlQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLG-----QFGLIKG-KSFPFEFDVRVP 352
Cdd:cd16151 205 ----EYFPDMV--------AYMDKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPitsrtNGREVRGgKGKTTDAGTHVP 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442619385 353 FLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQ--HMDGRSILPLLLSRNRAVRDNW 411
Cdd:cd16151 273 LIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLPEdyPLDGRSFAPQLLGKTGSPRREW 334
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-398 |
1.09e-39 |
|
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: 148.16 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ---------DVELgslnFMPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMY-----VHNHMVFTN 119
Cdd:cd16149 1 PNILFILTDDQgpwalgcygNSEA----VTPNLDRLAAEG-VRFENFFCTSPVCSPARASLLTGRMpsqhgIHDWIVEGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 120 NDNCSSP-QWQATHETrsYATYLSNAGYRTGYFGKylnkyngsyippgwreWgglimnskyynysinlngqkikHgfdya 198
Cdd:cd16149 76 HGKTKKPeGYLEGQTT--LPEVLQDAGYRCGLSGK----------------W----------------------H----- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 199 kdyypdlIANDSIAFLRSSKQQNqrKPVLLTMSFPAPHGPEdsapQYshlffnvtthhtpsydhapnpdkqwilrvtepm 278
Cdd:cd16149 111 -------LGDDAADFLRRRAEAE--KPFFLSVNYTAPHSPW----GY--------------------------------- 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 279 qpvhkrftnllmtkrLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGlIKGK---SFP---FEFDVRVP 352
Cdd:cd16149 145 ---------------FAAVTGVDRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHG-IWGKgngTFPlnmYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 442619385 353 FLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMD--GRSILP 398
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPADPRlpGRSFAD 257
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
53-409 |
3.31e-39 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 152.90 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDVELGSLNFMPR----TLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSspqW 128
Cdd:PRK13759 6 KPNIILIMVDQMRGDCLGCNGNKAvetpNLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHGRVGYGDVVP---W 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 129 QATHETrsyATYLSNAGYRTGYFGK--------------------YLN---KYNGS-------YIPPGWREWGGLimNSK 178
Cdd:PRK13759 83 NYKNTL---PQEFRDAGYYTQCIGKmhvfpqrnllgfhnvllhdgYLHsgrNEDKSqfdfvsdYLAWLREKAPGK--DPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 179 YYNYSINLNGQKIKhGFDYAKDYYP-DLIANDSIAFLRsskQQNQRKPVLLTMSFPAPHGPEDSaPQYshlFFNVtthht 257
Cdd:PRK13759 158 LTDIGWDCNSWVAR-PWDLEERLHPtNWVGSESIEFLR---RRDPTKPFFLKMSFARPHSPYDP-PKR---YFDM----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 258 psYDHAPNPD---KQWilRVTEPMQP-------VHKRFTNLLMTKRLQ----TLQSVDVAVERVYNELKELGELDNTYIV 323
Cdd:PRK13759 225 --YKDADIPDphiGDW--EYAEDQDPeggsidaLRGNLGEEYARRARAayygLITHIDHQIGRFLQALKEFGLLDNTIIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 324 YTSDHGYHLGQFGLIKgKSFPFEFDVRVPFLIRGPG----IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPL 399
Cdd:PRK13759 301 FVSDHGDMLGDHYLFR-KGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDDVDGRSLKNL 379
|
410
....*....|
gi 442619385 400 LLSRNRAVRD 409
Cdd:PRK13759 380 IFGQYEGWRP 389
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
54-426 |
3.09e-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: 293762 [Multi-domain] Cd Length: 395 Bit Score: 145.04 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDqdVELGSLNFMPRTLRL-------LRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSSP 126
Cdd:cd16143 1 PNIVIILADD--LGYGDISCYNPDSKIptpnidrLAAEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRSRLKGGVLGGFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 QWQAThETRSYATYLSNAGYRTGYFGKY---LNKY--NGSYIPPGWREWgglimnskyYNYSINLNGQKIKHGFDYakdY 201
Cdd:cd16143 79 PLIEP-DRVTLAKMLKQAGYRTAMVGKWhlgLDWKkkDGKKAATGTGKD---------VDYSKPIKGGPLDHGFDY---Y 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 202 Y-------PDLIANDSIAFLRSSKQQNqrKPVLLTMSFPAPHGPedsapqyshlffnvtthHTPSydhapnpdKQWILRV 274
Cdd:cd16143 146 FgipasevLPTLTDKAVEFIDQHAKKD--KPFFLYFALPAPHTP-----------------IVPS--------PEFQGKS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 275 TepmqpvhkrftnllMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG-------YHLGQFGLIK------GK 341
Cdd:cd16143 199 G--------------AGPYGDFVYELDWVVGRILDALKELGLAENTLVIFTSDNGpspyadyKELEKFGHDPsgplrgMK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 342 SFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQH--MDGRSILPLLLSRNRAVRdnwpDSFLIE 418
Cdd:cd16143 265 ADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLPDNaaEDSFSFLPALLGPKKQEV----RESLVH 340
|
....*...
gi 442619385 419 SSGRRETA 426
Cdd:cd16143 341 HSGNGSFA 348
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
79-440 |
6.24e-37 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 145.48 E-value: 6.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 79 RLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSSpqwqathETRSYATYLSNAGYRTGYFGKylnky 158
Cdd:cd16028 31 RLAAEG-VRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGTPLDA-------RHLTLALELRKAGYDPALFGY----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 159 nGSYIP-PGWREWGGLIMNSKYYnysinlngqkIKHGFDYAK--DYYPD------LIANDSIAFLRSSkqqnQRKPVLLT 229
Cdd:cd16028 98 -TDTSPdPRGLAPLDPRLLSYEL----------AMPGFDPVDrlDEYPAedsdtaFLTDRAIEYLDER----QDEPWFLH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 230 MSFPAPHGP-EDSAPqYSHLFFN-----VTTHHTPSYDHAPNPDKQWILRVTEPMQPVHKRFTNLLMTKR-LQTLQS--- 299
Cdd:cd16028 163 LSYIRPHPPfVAPAP-YHALYDPadvppPIRAESLAAEAAQHPLLAAFLERIESLSFSPGAANAADLDDEeVAQMRAtyl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 300 -----VDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIkGKSFPFEFDVRVPFLIRGPGIQAS----KVVNEIV 370
Cdd:cd16028 242 gliaeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWLW-GKDGFFDQAYRVPLIVRDPRREADatrgQVVDAFT 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619385 371 LNVDLAPTFLDMGGVPTPQHMDGRSILPLLlsrNRAVRDNWPDSFLIE------SSGRRETAEQIAESRARLQIER 440
Cdd:cd16028 321 ESVDVMPTILDWLGGEIPHQCDGRSLLPLL---AGAQPSDWRDAVHYEydfrdvSTRRPQEALGLSPDECSLAVIR 393
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
54-421 |
8.31e-37 |
|
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: 141.95 E-value: 8.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDdqdvELGSLnFMP-------RT--LRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFtnnDNCS 124
Cdd:cd16032 1 PNILLIMAD----QLTAA-ALPaygntvvKTpnLDRLAARGVVFDNAYCNSPLCAPSRASMMTGRLPSRIGAY---DNAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 125 spQWQAthETRSYATYLSNAGYRTGYFGKylnkyngsyippgwrewggliMNskyynysinLNGQKIKHGFDYakDyypD 204
Cdd:cd16032 73 --EFPA--DIPTFAHYLRAAGYRTALSGK---------------------MH---------FVGPDQLHGFDY--D---E 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 LIANDSIAFLRSSKQQNQRKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHH---TPSYdhapnpdkqwilrvtepmqpv 281
Cdd:cd16032 114 EVAFKAVQKLYDLARGEDGRPFFLTVSFTHPHDPYVIPQEYWDLYVRRARRAyygMVSY--------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 282 hkrftnllmtkrlqtlqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFpFEFDVRVPFLIRGPGIQ 361
Cdd:cd16032 173 ------------------VDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWYKMSF-FEGSARVPLIISAPGRF 233
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619385 362 ASKVVNEIVLNVDLAPTFLDMGGVPTPQH---MDGRSILPLLLSRnravRDNWPDSFLIESSG 421
Cdd:cd16032 234 APRRVAEPVSLVDLLPTLVDLAGGGTAPHvppLDGRSLLPLLEGG----DSGGEDEVISEYLA 292
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
54-418 |
8.75e-36 |
|
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: 142.52 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVEL----GSLNFMPRTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNNDNCSSpqwq 129
Cdd:cd16156 1 KQFIFIMTDTQRWDMvgcyGNKAMKTPNLDRLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHTNGSWTNCMALGD---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 130 athETRSYATYLSNAGYRTGYFGKY-LN--KYNGSYI-PPGWRE--WGGLIM---------NSKYYNYSINLNGQKIKHG 194
Cdd:cd16156 77 ---NVKTIGQRLSDNGIHTAYIGKWhLDggDYFGNGIcPQGWDPdyWYDMRNyldelteeeRRKSRRGLTSLEAEGIKEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 195 FDYAKDyypdlIANDSIAFLrsskQQNQRKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHHTPS-YDHAPN-PDKQWIL 272
Cdd:cd16156 154 FTYGHR-----CTNRALDFI----EKHKDEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENaYDDLENkPLHQRLW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 273 RVTEPmQPVHKRFTnLLMTKRLQTLQSVDVAVERVYNELKElgELDNTYIVYTSDHGYHLGQFGLI-KGKSFpFEFDVRV 351
Cdd:cd16156 225 AGAKP-HEDGDKGT-IKHPLYFGCNSFVDYEIGRVLDAADE--IAEDAWVIYTSDHGDMLGAHKLWaKGPAV-YDEITNI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619385 352 PFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLlsRNRAVRDNwpDSFLIE 418
Cdd:cd16156 300 PLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKVLEGESILATI--EDPEIPEN--RGVFVE 363
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
53-411 |
1.52e-35 |
|
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: 140.27 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDD---QDVE-LGSLNFMPrTLRLLRDGGAEFRHAYTTtPMCCPARSSLLTGMYVH-NHMVFTNNDNCSSPQ 127
Cdd:cd16025 2 RPNILLILADDlgfSDLGcFGGEIPTP-NLDALAAEGLRFTNFHTT-ALCSPTRAALLTGRNHHqVGMGTMAELATGKPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 128 WQA--THETRSYATYLSNAGYRTGYFGKylnkyngsyippgwreWgglimnskyynysinlngqkikH-GFDyakDYY-P 203
Cdd:cd16025 80 YEGylPDSAATIAEVLKDAGYHTYMSGK----------------W----------------------HlGPD---DYYsT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 204 DLIANDSIAFLRssKQQNQRKPVLLTMSFPAPHGPedsapqyshlffnvttHHTPS---------YDH------------ 262
Cdd:cd16025 119 DDLTDKAIEYID--EQKAPDKPFFLYLAFGAPHAP----------------LQAPKewidkykgkYDAgwdalreerler 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 263 -------------APNPD--KQWilrvtEPMQPVHKRftnlLMTKRLQT----LQSVDVAVERVYNELKELGELDNTYIV 323
Cdd:cd16025 181 qkelglipadtklTPRPPgvPAW-----DSLSPEEKK----LEARRMEVyaamVEHMDQQIGRLIDYLKELGELDNTLII 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 324 YTSDHG--YHLG--QFG---LIKGKSFPFEFDVRVPFLIRGPGIQASK--VVNEIVLNVDLAPTFLDMGGVPTPQH---- 390
Cdd:cd16025 252 FLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPKGIKAKggIRHQFAHVIDIAPTILELAGVEYPKTvngv 331
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 442619385 391 ----MDGRSILPLL---------------LSRNRAVR-DNW 411
Cdd:cd16025 332 pqlpLDGVSLLPTLdgaaapsrrrtqyfeLFGNRAIRkGGW 372
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-398 |
6.18e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 134.60 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDdqdvelgSLNF------------MPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFtnnd 121
Cdd:cd16148 1 MNVILIVID-------SLRAdhlgcygydrvtTPNLDRLAAEG-VVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVW---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 122 ncsspQWQATHETRSYATYLSNAGYRTGYFGkylnkyNGSYIPPGWrewgGLimnSKYYNYSINLNGQkikHGFDYAKDY 201
Cdd:cd16148 69 -----GGPLEPDDPTLAEILRKAGYYTAAVS------SNPHLFGGP----GF---DRGFDTFEDFRGQ---EGDPGEEGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 202 YPDLIANDS-IAFLRSskqqnqrkpvlltmsfpapHGPEDsaPQYSHLFFNVTthHTPS-YDhapnpdkqwilrvtepmq 279
Cdd:cd16148 128 ERAERVTDRaLEWLDR-------------------NADDD--PFFLFLHYFDP--HEPYlYD------------------ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 280 pvhkrftNLLMTkrlqtlqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPF-EFDVRVPFLIRGP 358
Cdd:cd16148 167 -------AEVRY--------VDEQIGRLLDKLKELGLLEDTLVIVTSDHGEEFGEHGLYWGHGSNLyDEQLHVPLIIRWP 231
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 442619385 359 GIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILP 398
Cdd:cd16148 232 GKEPGKRVDALVSHIDIAPTLLDLLGVEPPDYSDGRSLLP 271
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
53-409 |
1.83e-33 |
|
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: 133.84 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQ---DVE-LGS-LNFMPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMY-----VHNHMVFTNNDN 122
Cdd:cd16026 1 KPNIVVILADDLgygDLGcYGSpLIKTPNIDRLAAEG-VRFTDFYAAAPVCSPSRAALLTGRYpvrvgLPGVVGPPGSKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 123 CSSPQwqathETrSYATYLSNAGYRTGYFGKYLNKYNGSYIPP--GWREWGGlIMNS----KYYNYSINLNGQKIKHGFD 196
Cdd:cd16026 80 GLPPD-----EI-TIAEVLKKAGYRTALVGKWHLGHQPEFLPTrhGFDEYFG-IPYSndmwPFPLYRNDPPGPLPPLMEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 197 YAKDYYPD-------LIANDSIAFLRsskqQNQRKPVLLTMSFPAPHGPEDSAPQyshlfFNVTTHHTPSYDhapnpdkq 269
Cdd:cd16026 153 EEVIEQPAdqssltqRYTDEAVDFIE----RNKDQPFFLYLAHTMPHVPLFASEK-----FKGRSGAGLYGD-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 270 wilrvtepmqpvhkrftnllmtkrlqTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG------YHLGQFGLIKG-KS 342
Cdd:cd16026 216 --------------------------VVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleygGHGGSAGPLRGgKG 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 343 FPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQH--MDGRSILPLLLSRNRAVRD 409
Cdd:cd16026 270 TTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLPEDrvIDGKDISPLLLGGSKSPPH 339
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
53-409 |
2.29e-30 |
|
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: 125.62 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDV-----------ELGSLNFMPRTlrllrdgGAEFRHAYTTTPMCCPARSSLLTGMY-VHNHM----- 115
Cdd:cd16160 1 KPNIVLFFADDMGYgdlasyghptqERGPIDDMAAE-------GIRFTQAYSADSVCTPSRAALLTGRLpIRSGMyggtr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 116 VFTNNDNCSSPQWQAThetrsYATYLSNAGYRTGYFGKY---LNKYN---GSYIP------------P---GWR--EWGG 172
Cdd:cd16160 74 VFLPWDIGGLPKTEVT-----MAEALKEAGYTTGMVGKWhlgINENNhsdGAHLPshhgfdfvgtnlPftnSWAcdDTGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 173 LI---MNSK---YYNYSINlnGQKIKHgfdyakDYYPDLIANDSIAFLrsskQQNQRKPVLLTMSFPAPHgpedsAPQYS 246
Cdd:cd16160 149 HVdfpDRSAcflYYNDTIV--EQPIQH------EHLTETLVGDAKSFI----EDNQENPFFLYFSFPQTH-----TPLFA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 247 HlffnvtthhtpsydhapnpdkqwilrvtepmqpvhKRFTNLLMTKRL-QTLQSVDVAVERVYNELKELGELDNTYIVYT 325
Cdd:cd16160 212 S-----------------------------------KRFKGKSKRGRYgDNINEMSWAVGEVLDTLVDTGLDQNTLVFFL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 326 SDHGYHL------GQFGLIKG-KSFPFEFDVRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGG--VPTPQHMDGRSI 396
Cdd:cd16160 257 SDHGPHVeyclegGSTGGLKGgKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGgtLPTDRIYDGLSI 336
|
410
....*....|...
gi 442619385 397 LPLLLSRNRAVRD 409
Cdd:cd16160 337 TDLLLGEADSPHD 349
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
54-410 |
1.80e-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: 119.19 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQ---DVEL-GSLNFMPRTLRLLRDGGAEFRHAYTTtPMCCPARSSLLTGMY-VHNHMVFTNNDNcSSPQW 128
Cdd:cd16029 1 PHIVFILADDLgwnDVGFhGSDQIKTPNLDALAADGVILNNYYVQ-PICTPSRAALMTGRYpIHTGMQHGVILA-GEPYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 129 QATHETrSYATYLSNAGYRTGYFGKY-LNKYNGSYIPPGwR-------EWGGLI-----MNSKYYNYSINLNGQKIKHGF 195
Cdd:cd16029 79 LPLNET-LLPQYLKELGYATHLVGKWhLGFYTWEYTPTN-RgfdsfygYYGGAEdyythTSGGANDYGNDDLRDNEEPAW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 196 DYAKDYYPDLIANDSIAFLRsskQQNQRKPVLLTMSFPAPHGPEDSAPQYSHLFFNVTTHHTPsydhapnpdkqwilrvt 275
Cdd:cd16029 157 DYNGTYSTDLFTDRAVDIIE---NHDPSKPLFLYLAFQAVHAPLQVPPEYADPYEDKFAHIKD----------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 276 epmqpvHKRFTNLLMTKRLqtlqsvDVAVERVYNELKELGELDNTYIVYTSDHGyhlGQFGLIK---------GKSFPFE 346
Cdd:cd16029 217 ------EDRRTYAAMVSAL------DESVGNVVDALKAKGMLDNTLIVFTSDNG---GPTGGGDggsnyplrgGKNTLWE 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619385 347 FDVRVPFLIRGPGIQASK--VVNEIVLNVDLAPTFLDMGG--VPTPQHMDGRSILPLLLSRNRAVRDN 410
Cdd:cd16029 282 GGVRVPAFVWSPLLPPKRgtVSDGLMHVTDWLPTLLSLAGgdPDDLPPLDGVDQWDALSGGAPSPRTE 349
|
|
| DUF3740 |
pfam12548 |
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and ... |
637-793 |
1.72e-27 |
|
Sulfatase protein; This domain family is found in eukaryotes, and is typically between 144 and 173 amino acids in length. The family is found in association with pfam00884.
Pssm-ID: 463628 Cd Length: 142 Bit Score: 108.97 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 637 GRRRNKR--------EVFHTEL-----PDEMEELLDLHQVVDQlvDHTHRskrdlpassnetiaqviqqiqstleilELK 703
Cdd:pfam12548 5 VRTRQKRslsvefegEVYDIDLeeeyqPLEPRNLLKRHARDDG--EEGEE---------------------------GEE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 704 FNEHELHASNSSGNSYERGEKYTksggHRCFVDATtAKVNCSNVIYDDEKTWRTSRTQIDMLIKLLKDKIGKLKEMKKQL 783
Cdd:pfam12548 56 SSGTGSKRDSSNSVGPPASVKVT----HRCYILAN-DTVKCDNVLYKSLQAWKDHKLHIDHEIETLKDKIKNLKEVKGHL 130
|
170
....*....|
gi 442619385 784 RESNKQALAA 793
Cdd:pfam12548 131 KERRPEECDC 140
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
54-411 |
3.31e-27 |
|
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: 114.94 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDqdveLGSLNF------------MPRTLRLLRDGgAEFRHAYTTtPMCCPARSSLLTGMYVhnhmvftNND 121
Cdd:cd16142 1 PNILVILGDD----IGWGDLgcygggigrgapTPNIDRLAKEG-LRFTSFYVE-PSCTPGRAAFITGRHP-------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 122 NCSSPQWQA-----THETRSYATYLSNAGYRTGYFGKylnkyngsyippgWRewggliMNSKYYNYSINlngqkikHGFD 196
Cdd:cd16142 68 GLTTVGLPGspgglPPWEPTLAELLKDAGYATAQFGK-------------WH------LGDEDGRLPTD-------HGFD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 197 YAKDYYP----DLIANDSIAFLRSSKQQNqrKPvlltmsfpaphgpedsapqyshlFF---NVTTHHTPSYdhaPNPDkq 269
Cdd:cd16142 122 EFYGNLYhtidEEIVDKAIDFIKRNAKAD--KP-----------------------FFlyvNFTKMHFPTL---PSPE-- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 270 wilrvtepmqpvhkrFTNLLMTKRLQ--TLQSVDVAVERVYNELKELGELDNTYIVYTSDHG-----YHLGQFGLIKG-K 341
Cdd:cd16142 172 ---------------FEGKSSGKGKYadSMVELDDHVGQILDALDELGIADNTIVIFTTDNGpeqdvWPDGGYTPFRGeK 236
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442619385 342 SFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTP--------QHMDGRSILPLLLSRNRAVRDNW 411
Cdd:cd16142 237 GTTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPkdkllgkdRHIDGVDQSPFLLGKSEKSRRSE 315
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
53-396 |
5.82e-27 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293772 [Multi-domain] Cd Length: 282 Bit Score: 112.08 E-value: 5.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDVE-LGSLN---FMPRTLRL----------LRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFT 118
Cdd:cd16153 1 KPNILWIITDDQRVDsLSCYNnahTGKSESRLgyvespnidaLAAEGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 119 NndncsSPQWQATHE-TRSYATYLSNAGYRTGYFGK--------YLNKYNGSYIPPgwreWGglimnskyynysinlngq 189
Cdd:cd16153 81 F-----EAAHPALDHgLPTFPEVLKKAGYQTASFGKshleafqrYLKNANQSYKSF----WG------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 190 KIKHGFDyakdyypdliandsiaflrsskqqnQRKPVLLTMSFPAPHgpedsapqyshlffnvtthhTPSYdhapnPDKQ 269
Cdd:cd16153 134 KIAKGAD-------------------------SDKPFFVRLSFLQPH--------------------TPVL-----PPKE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 270 WilrvtepmqpvHKRFTNLLMTKRlqtlqsVDVAVERVYNELKELGEL---DNTYIVYTSDHGYHLGQFGlIKGKSFPFE 346
Cdd:cd16153 164 F-----------RDRFDYYAFCAY------GDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQG-ILAKFTFWP 225
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 442619385 347 FDVRVPFLIRGPG---IQASKVVNEIVLNVDLAPTFLDMGGVP--TPQHMDGRSI 396
Cdd:cd16153 226 QSHRVPLIVVSSDklkAPAGKVRHDFVEFVDLAPTLLAAAGVDvdAPDYLDGRDL 280
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-409 |
3.05e-26 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 112.06 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVE------LGS-LNFMPrTLRLLRDGGAEFRHAYTTtPMCCPARSSLLTGMYVHNHMVFTNNDNCSSP 126
Cdd:cd16154 1 PNILLIIADDQGLDssaqysLSSdLPVTP-TLDSLANSGIVFDNLWAT-PACSPTRATILTGKYGFRTGVLAVPDELLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 qwqatHET--RSYATYLSNAGYRTGYFGKYL--NKYNGSYIPPGWREWGGLIMN--SKYYNYSINLNGQKIKHGfDYAKD 200
Cdd:cd16154 79 -----EETllQLLIKDATTAGYSSAVIGKWHlgGNDNSPNNPGGIPYYAGILGGgvQDYYNWNLTNNGQTTNST-EYATT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 201 YypdlIANDSIAFLrsskqQNQRKPVLLTMSFPAPHGPedsapqyshlfFNVTTHHTPSYDHAPnpdkqwilrvTEPMQP 280
Cdd:cd16154 153 K----LTNLAIDWI-----DQQTKPWFLWLAYNAPHTP-----------FHLPPAELHSRSLLG----------DSADIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 281 VHKRFTNLLMtkrlqtLQSVDVAVERVYNELKElGELDNTYIVYTSDHG---------YHLGQfglikGKSFPFEFDVRV 351
Cdd:cd16154 203 ANPRPYYLAA------IEAMDTEIGRLLASIDE-EERENTIIIFIGDNGtpgqvvdlpYTRNH-----AKGSLYEGGINV 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 442619385 352 PFLIRGPGI-QASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16154 271 PLIVSGAGVeRANERESALVNATDLYATIAELAGVDAAEIHDSVSFKPLLSDVNASTRQ 329
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
54-411 |
3.65e-25 |
|
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: 108.78 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTD-----------DQDVELGSLNFMprtlrllRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFtNNDN 122
Cdd:cd16171 1 PNVVMVMSDsfdgrltfrpgNQVVDLPYINFM-------KQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESW-NNYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 123 CSSPqwqathetrSYATY---LSNAGYRTGYFGKyLNKYNGSY------------IPPGWREWGglimnskyyNYSINLN 187
Cdd:cd16171 73 GLDP---------NYPTWmdrLEKHGYHTQKYGK-LDYTSGHHsvsnrveawtrdVPFLLRQEG---------RPTVNLV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 188 GQKiKHGFDYAKDYYpdlIANDSIAFLRSSKQqNQRKPVLLTMSFPAPHgpedsapqyshlffnvtthhtpsydhaPNPd 267
Cdd:cd16171 134 GDR-STVRVMLKDWQ---NTDKAVHWIRKEAP-NLTQPFALYLGLNLPH---------------------------PYP- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 268 kqwilrvTEPMQPvhkrftNLLMTKRLQTL-----QSVDVAVERVYNELKELGELDNTYIVYTSDHG---YHLGQFGlik 339
Cdd:cd16171 181 -------SPSMGE------NFGSIRNIRAFyyamcAETDAMLGEIISALKDTGLLDKTYVFFTSDHGelaMEHRQFY--- 244
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442619385 340 gKSFPFEFDVRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLL------SRNRAVRDNW 411
Cdd:cd16171 245 -KMSMYEGSSHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQPQNLSGYSLLPLLSessikeSPSRVPHPDW 321
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
54-409 |
2.10e-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: 293769 [Multi-domain] Cd Length: 423 Bit Score: 101.54 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDVE-LGSLN----FMPRTLRLLRDGgAEFRHAYTTTPMCCPARSSLLTGMYVH-------NHMVFTNND 121
Cdd:cd16150 1 PNIVIFVADQLRADsLGHLGnpaaVTPNLDALAAEG-VRFSNAYCQNPVCSPSRCSFLTGWYPHvnghrtlHHLLRPDEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 122 NcsspqwqathetrsYATYLSNAGYRTGYFGKylnkyNGSYIPPGWREwgglimnskyynysinlngqkikhgfDYAKDy 201
Cdd:cd16150 80 N--------------LLKTLKDAGYHVAWAGK-----NDDLPGEFAAE--------------------------AYCDS- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 202 yPDLIANDSIAFLRsskQQNQRKPVLLTMSFPAPHGP-EDSAPQYShlffnvtthhtpSYDHAPNPDKqwILRVTEPMQP 280
Cdd:cd16150 114 -DEACVRTAIDWLR---NRRPDKPFCLYLPLIFPHPPyGVEEPWFS------------MIDREKLPPR--RPPGLRAKGK 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 281 V----HKRFTNL--LMTKRLQTLQSV--------DVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKgkSFPFE 346
Cdd:cd16150 176 PsmleGIEKQGLdrWSEERWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGLVE--KWPNT 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442619385 347 FD---VRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQHMDGRSILPLLLSRNRAVRD 409
Cdd:cd16150 254 FEdclTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHFGRSLLPVLAGETEEHRD 319
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
53-400 |
7.01e-21 |
|
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: 97.74 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDV-ELGSlnFMPRTLR-----LLRDGGAEFRHAYTTTPMCCPARSSLLTGMY--------VHNHMVFT 118
Cdd:cd16159 1 KPNIVLFMADDLGIgDVGC--FGNDTIRtpnidRLAKEGVKLTHHLAAAPLCTPSRAAFLTGRYpirsgmasSHGMRVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 119 NNdncSSPQWQATHETrSYATYLSNAGYRTGYFGKY----------------LNK-----------------------YN 159
Cdd:cd16159 79 FT---ASSGGLPPNET-TFAEVLKQQGYSTALIGKWhlglhcesrndfchhpLNHgfdyfyglpltnlkdcgdgsngeYD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 160 GSYIPP------------------------GWRE--------------WGGLIMNSKYYNYSINLNGQKIKHGFDYakdy 201
Cdd:cd16159 155 LSFDPLfplltafvlitaltiflllylgavSKRFfvfllilsllfislFFLLLITNRYFNCILMRNHEVVEQPMSL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 202 yPDL---IANDSIAFLrsskQQNQRKPVLLTMSFPAPHGPEDSAPqyshLFFNVTTHHTpsYDHApnpdkqwilrVTEpm 278
Cdd:cd16159 231 -ENLtqrLTKEAISFL----ERNKERPFLLVMSFLHVHTALFTSK----KFKGRSKHGR--YGDN----------VEE-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 279 qpvhkrftnllmtkrlqtlqsVDVAVERVYNELKELGELDNTYIVYTSDHGYHL----------GQFGLIKG--KSFPFE 346
Cdd:cd16159 288 ---------------------MDWSVGQILDALDELGLKDNTFVYFTSDNGGHLeeisvggeygGGNGGIYGgkKMGGWE 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 442619385 347 FDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTP--QHMDGRSILPLL 400
Cdd:cd16159 347 GGIRVPTIVRWPGvIPPGSVIDEPTSLMDIFPTVAALAGAPLPsdRIIDGRDLMPLL 403
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
54-409 |
2.27e-20 |
|
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: 95.97 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDDQDV-ELGSLNFmPRT----LRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMY-VHNHM---VFTNNDNCS 124
Cdd:cd16158 2 PNIVLLFADDLGYgDLGCYGH-PSSstpnLDRLAANGLRFTDFYSSSPVCSPSRAALLTGRYqVRSGVypgVFYPGSRGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 125 SPqwqatHETRSYATYLSNAGYRTGYFGKY---LNKyNGSYIPPgwrewgglimnskyynysinlngqkiKHGFD----- 196
Cdd:cd16158 81 LP-----LNETTIAEVLKTVGYQTAMVGKWhlgVGL-NGTYLPT--------------------------HQGFDhylgi 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 197 -YAKD---------YYPD---------------LIANDSIaflrssKQQnqrkPVLLT------MSFpAPHGPEDSAPQY 245
Cdd:cd16158 129 pYSHDqgpcqnltcFPPNipcfggcdqgevpcpLFYNESI------VQQ----PVDLLtleeryAKF-AKDFIADNAKEG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 246 SHLFFNVTTHHTpsydHAPnpdkqwilrvtepmQPVHKRFTNLLMTKRL-QTLQSVDVAVERVYNELKELGELDNTYIVY 324
Cdd:cd16158 198 KPFFLYYASHHT----HYP--------------QFAGQKFAGRSSRGPFgDALAELDGSVGELLQTLKENGIDNNTLVFF 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 325 TSDHGYHL------GQFGLIK-GKSFPFEFDVRVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTPQ-HMDGRSI 396
Cdd:cd16158 260 TSDNGPSTmrksrgGNAGLLKcGKGTTYEGGVREPAIAYWPGRIKPGVTHELASTLDILPTIAKLAGAPLPNvTLDGVDM 339
|
410
....*....|...
gi 442619385 397 LPLLLSRNRAVRD 409
Cdd:cd16158 340 SPILFEQGKSPRQ 352
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
54-381 |
4.44e-20 |
|
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: 90.56 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTDD-QDVELG-SLNFMPRT--LRLLRDGGAEFRHaYTTTPMC--CPARSSLLTGMYVHNHMVFTNNDNCSSPQ 127
Cdd:cd00016 1 KHVVLIVLDGlGADDLGkAGNPAPTTpnLKRLASEGATFNF-RSVSPPTssAPNHAALLTGAYPTLHGYTGNGSADPELP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 128 WQATHETRSYATY---LSNAGYRTGYFGkylnkyngsyippgwrewgglimnskyynysinlngqkikhgfdyakdyypd 204
Cdd:cd00016 80 SRAAGKDEDGPTIpelLKQAGYRTGVIG---------------------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 liandsiaFLRSSKQQNQRKPVLLTMSFPAPHGPedsapqySHLFfnvtTHHTPSYDhapnpdkqwilrvtepmqpvhkr 284
Cdd:cd00016 108 --------LLKAIDETSKEKPFVLFLHFDGPDGP-------GHAY----GPNTPEYY----------------------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 285 ftnllmtkrlQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG---YHLGQFGLIKGKSFPFEFDVRVPFLIRGPGIQ 361
Cdd:cd00016 146 ----------DAVEEIDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGPGVK 215
|
330 340
....*....|....*....|
gi 442619385 362 ASKVVNEIVLNVDLAPTFLD 381
Cdd:cd00016 216 KGGVKHELISQYDIAPTLAD 235
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
54-382 |
6.02e-19 |
|
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: 88.51 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILIL-----TDDQDVELGSLNFMPrTLRLLRDGGAEFRHAYTTTPMCCPARS--SLLTGMYvhnhmvfTNNDNCSSP 126
Cdd:cd16015 1 PNVIVILlesfsDPYIDKDVGGEDLTP-NLNKLAKEGLYFGNFYSPGFGGGTANGefEVLTGLP-------PLPLGSGSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 QWQATHETRSYATYLSNAGYRTGYFGkylnkyngsyipPGWREWGGLimnSKYYNysinlngqkiKHGFD--YAKDYYPD 204
Cdd:cd16015 73 TLYKLNPLPSLPSILKEQGYETIFIH------------GGDASFYNR---DSVYP----------NLGFDefYDLEDFPD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 205 LI-------ANDSIAFLRSSKQ--QNQRKPVLLTMsfpaphgpedsapqyshlfFNVTTHHtPsYDHAPNPDKQwilrvt 275
Cdd:cd16015 128 DEketngwgVSDESLFDQALEEleELKKKPFFIFL-------------------VTMSNHG-P-YDLPEEKKDE------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 276 epmqPVHKRFTNLLMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGYHLGQFGLIKGKSFPFEFdvRVPFLI 355
Cdd:cd16015 181 ----PLKVEEDKTELENYLNAIHYTDKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLI 254
|
330 340
....*....|....*....|....*..
gi 442619385 356 RGPGIQASKVVNEIVLNVDLAPTFLDM 382
Cdd:cd16015 255 YSPGLKKPKKIDRVGSQIDIAPTLLDL 281
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
46-438 |
8.30e-19 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 91.64 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 46 SNSARERRPNIILIL-----TDDQDVELGSLNFMPrTLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYV--HNHMVFT 118
Cdd:COG1368 227 NPFGPAKKPNVVVILlesfsDFFIGALGNGKDVTP-FLDSLAKESLYFGNFYSQGGRTSRGEFAVLTGLPPlpGGSPYKR 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 119 NNDNcsspqwqathETRSYATYLSNAGYRTGYFgkylnkYNGsyippgwrewgglimNSKYYNYSINLNGQkikhGFD-- 196
Cdd:COG1368 306 PGQN----------NFPSLPSILKKQGYETSFF------HGG---------------DGSFWNRDSFYKNL----GFDef 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 197 YAKDYYPDLIAN-----DSIAFLRSSKQQNQRKpvlltmsfpaphgpedsAPQYSHLFFnvTTHHTPsYDhAPNPDKqwi 271
Cdd:COG1368 351 YDREDFDDPFDGgwgvsDEDLFDKALEELEKLK-----------------KPFFAFLIT--LSNHGP-YT-LPEEDK--- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 272 lRVTEpmqpvhkrFTNLLMTKRLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGyhlgqfGLIKGKSfPFEFDV-- 349
Cdd:COG1368 407 -KIPD--------YGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHG------PRSPGKT-DYENPLer 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 350 -RVPFLIRGPGIQASKVVNEIVLNVDLAPTFLDMGGVPTP-QHMDGRSILpLLLSRNRAVRDNW---PDSFLIESSGRR- 423
Cdd:COG1368 471 yRVPLLIYSPGLKKPKVIDTVGSQIDIAPTLLDLLGIDYPsYYAFGRDLL-SPDTDPFAFRNGGfitDDYVYVLKTGELt 549
|
410
....*....|....*.
gi 442619385 424 -ETAEQIAESRARLQI 438
Cdd:COG1368 550 eEDKELEEEALAYLQL 565
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
53-401 |
1.83e-18 |
|
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
Pssm-ID: 293776 [Multi-domain] Cd Length: 466 Bit Score: 89.83 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDV-ELGSLNFMPR---TLRLLRDGGAEFRHAYTTTPMCCPARSSLLTGMYVHNHMVFTNND---NCSS 125
Cdd:cd16157 1 KPNIILMLMDDMGWgDLGVFGEPSRetpNLDRMAAEGMLFTDFYSANPLCSPSRAALLTGRLPIRNGFYTTNAharNAYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 126 PQWQATHETRS---YATYLSNAGYRTGYFGKYLNKYNGSYIP--PGWREWGGL----------------------IMNSK 178
Cdd:cd16157 81 PQNIVGGIPDSeilLPELLKKAGYRNKIVGKWHLGHRPQYHPlkHGFDEWFGApnchfgpydnkaypnipvyrdwEMIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 179 YY-NYSINLNGqkikhgfdyAKDYYPDLIANDSIAFLrsSKQQNQRKPVLLTMSFPAPHgpedsAPQYSHLFFNVTTHHT 257
Cdd:cd16157 161 YYeEFKIDKKT---------GESNLTQIYLQEALEFI--EKQHDAQKPFFLYWAPDATH-----APVYASKPFLGTSQRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 258 PSYDhapnpdkqwilrvtepmqpvhkrftnllmtkrlqTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG---YHLGQ 334
Cdd:cd16157 225 LYGD----------------------------------AVMELDSSVGKILESLKSLGIENNTFVFFSSDNGaalISAPE 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442619385 335 FG-----LIKGKSFPFEFDVRVPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTP--QHMDGRSILPLLL 401
Cdd:cd16157 271 QGgsngpFLCGKQTTFEGGMREPAIAWWPGhIKPGQVSHQLGSLMDLFTTSLALAGLPIPsdRAIDGIDLLPVLL 345
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
53-403 |
4.73e-17 |
|
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: 84.44 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 53 RPNIILILTDDQDVELGSLNFMPRT-----LRLLRDGGAEFRHAYTTTPMCCPARSSLLTG-MYVHNHMvfTNNDNCSSP 126
Cdd:cd16161 1 KPNFLLLFADDLGWGDLGANWAPNAiltpnLDKLAAEGTRFVDWYSAASVCSPSRASLMTGrLGLRNGV--GHNFLPTSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 127 QWQATHETrSYATYLSNAGYRTGYFGKYLNKYNGSYIPpgwrewgglimNSKYYNYSinlngqkikHGFDYAKD-YYPDL 205
Cdd:cd16161 79 GGLPLNET-TLAEVLRQAGYATGMIGKWHLGQREAYLP-----------NSRGFDYY---------FGIPFSHDsSLADR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 206 IANDSIAFLRSSKQQNQrkPVLLTMSFPAPHGPEDSAPqyshLFFNVTTHHTPSYDhapnpdkqwilrvtepmqpvhkrf 285
Cdd:cd16161 138 YAQFATDFIQRASAKDR--PFFLYAALAHVHVPLANLP----RFQSPTSGRGPYGD------------------------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 286 tnllmtkrlqTLQSVDVAVERVYNELKELGELDNTYIVYTSD---------------HGYHLGQFGLIKGKSFPFEFDVR 350
Cdd:cd16161 188 ----------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGSVAKASTWEGGHR 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 442619385 351 VPFLIRGPG-IQASKVVNEIVLNVDLAPTFLDMGGVPTPQH--MDGRSILPLLLSR 403
Cdd:cd16161 258 EPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPPGriYDGKDLSPVLFGG 313
|
|
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
940-989 |
8.14e-12 |
|
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: 68.35 E-value: 8.14e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 442619385 940 CMNANNNTYSCLRTINGTHNFLYCEFTTGLITFYNLTIDRFETINRAAGL 989
Cdd:cd16147 347 CGDSNNNTYKCVRTVDDTYNLLYFEWCTGFRELYDLTTDPYQLTNLAGDL 396
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
240-388 |
1.86e-08 |
|
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];
Pssm-ID: 442317 [Multi-domain] Cd Length: 603 Bit Score: 58.38 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 240 DSAPQYSHLFFNVTThhtPSYDHAPNPDKQWILRVTEPMQPVHKRFTNLLMTKRLQTLQSVDVAVERVYNELKELGELDN 319
Cdd:COG3083 379 SDRPWFSYLFLDAPH---AYSFPADYPKPFQPSEDCNYLALDNESDPTPFKNRYRNAVHYVDSQIGRVLDTLEQRGLLEN 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619385 320 TYIVYTSDHGYHL---GQFGLIKGKSFPfEFDVRVPFLIRGPGiQASKVVNEIVLNVDLAPTFL-DMGGVPTP 388
Cdd:COG3083 456 TIVIITADHGEEFnenGQNYWGHNSNFS-RYQLQVPLVIHWPG-TPPQVISKLTSHLDIVPTLMqRLLGVQNP 526
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
54-381 |
3.78e-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: 56.05 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 54 PNIILILTD--DQDvELGSLNFMPrTLRLLRDGGAEFRHAYTTTP-MCCPARSSLLTGMY------VHNHM-------VF 117
Cdd:cd16018 1 PPLIVISIDgfRWD-YLDRAGLTP-NLKRLAEEGVRAKYVKPVFPtLTFPNHYSIVTGLYpeshgiVGNYFydpktneEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 118 TNNDNCSSPQWQAThETrSYATyLSNAGYRTG-YF--GKyLNKYNGSYIPPGWREWgglimnSKYYNYSINLNGQKIKHG 194
Cdd:cd16018 79 SDSDWVWDPWWIGG-EP-IWVT-AEKAGLKTAsYFwpGS-EVAIIGYNPTPIPLGG------YWQPYNDSFPFEERVDTI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 195 FDYAKDYYPDLIandsiaflrsskqqnqrkpvllTMSFPAPhgpeDSApqySHlffnvtthhtpsyDHAPNpdkqwilrv 274
Cdd:cd16018 149 LEWLDLERPDLI----------------------LLYFEEP----DSA---GH-------------KYGPD--------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 275 tepmqpvHKRFTnllmtkrlQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHGY-----HlGQfglikgksFPFEFDV 349
Cdd:cd16018 178 -------SPEVN--------EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMtdvgtH-GY--------DNELPDM 233
|
330 340 350
....*....|....*....|....*....|..
gi 442619385 350 RVPFLIRGPGIQASKVVNEIvLNVDLAPTFLD 381
Cdd:cd16018 234 RAIFIARGPAFKKGKKLGPF-RNVDIYPLMCN 264
|
|
| COG3379 |
COG3379 |
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction ... |
353-400 |
6.05e-07 |
|
Predicted phosphohydrolase or phosphomutase, AlkP superfamily [General function prediction only];
Pssm-ID: 442606 [Multi-domain] Cd Length: 472 Bit Score: 53.37 E-value: 6.05e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442619385 353 FLIRGPGIQASKVVNEIVLnVDLAPTFLDMGGVPTPQHMDGRSILPLL 400
Cdd:COG3379 422 FLAAGPGIAPGARLEDADL-YDVAPTILALLGLPVPRDMDGRVLVEAF 468
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
47-329 |
1.71e-06 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 51.67 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 47 NSARERRPNIILILTD----DQdveLGSLNfMPrTLRLLRDGGAEFRHAYTTTP-MCCPARSSLLTGMY------VHNHM 115
Cdd:COG1524 17 AAAAPPAKKVVLILVDglraDL---LERAH-AP-NLAALAARGVYARPLTSVFPsTTAPAHTTLLTGLYpgehgiVGNGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 116 VFTNNDNCSSPQWQATHETRSYATY--------LSNAGYRTGYFGkylnkyngsyippgwreWGGLIMnSKYYNYSI--N 185
Cdd:COG1524 92 YDPELGRVVNSLSWVEDGFGSNSLLpvptiferARAAGLTTAAVF-----------------WPSFEG-SGLIDAARpyP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 186 LNGQKIKHGFDYAKDYypdlIANDSIAFLRsskqqnQRKPVLLTMSFPAPhgpeDSApqySHlffnvttHHTPSYDHApn 265
Cdd:COG1524 154 YDGRKPLLGNPAADRW----IAAAALELLR------EGRPDLLLVYLPDL----DYA---GH-------RYGPDSPEY-- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442619385 266 pdkqwilrvtepmqpvhkrftnllmtkrLQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG 329
Cdd:COG1524 208 ----------------------------RAALREVDAALGRLLDALKARGLYEGTLVIVTADHG 243
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
304-385 |
3.70e-06 |
|
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase; Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine Transferase catalyzes the modification of the lipid A headgroups by phosphoethanolamine (PEA) or 4-amino-arabinose residues. Lipopolysaccharides, also called endotoxins, protect bacterial pathogens from antimicrobial peptides and have roles in virulence. The PEA modified lipid A increases resistance to the cationic cyclic polypeptide antibiotic, polymyxin. Lipid A PEA transferases usually consist of a transmembrane domain anchoring the enzyme to the periplasmic face of the cytoplasmic membrane.
Pssm-ID: 293741 [Multi-domain] Cd Length: 288 Bit Score: 49.93 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 304 VERVYNELKELGEldNTYIVYTSDHGYHLGQFGLIK-GKSFPFEFDVRVPFLI--------RGPGIQASKVVNEIVLNVD 374
Cdd:cd16017 199 LSQIIERLKKKDK--DAALIYFSDHGESLGENGLYLhGAPYAPKEQYHVPFIIwssdsykqRYPVERLRANKDRPFSHDN 276
|
90
....*....|.
gi 442619385 375 LAPTFLDMGGV 385
Cdd:cd16017 277 LFHTLLGLLGI 287
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
300-397 |
1.15e-04 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 46.25 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 300 VDVAVERVYNELKELGeldntYIVY-TSDHG-----YHLGQFGLIKGKS-FPfefdvrVPFLIRGPGIQASKVVNEIVLN 372
Cdd:cd16010 412 VDECLGRIVEAVLENG-----GTLLiTADHGnaeemIDPETGGPHTAHTtNP------VPFIIVDPGLKRKLLKDGGLAD 480
|
90 100
....*....|....*....|....*
gi 442619385 373 VdlAPTFLDMGGVPTPQHMDGRSIL 397
Cdd:cd16010 481 V--APTILDLLGIEKPKEMTGKSLI 503
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
289-388 |
2.59e-04 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 44.09 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 289 LMTKRLQTLQSVdvaVERVYNELKELGELDNTYIVYTSDHGY-----HlgqfglikGKSFPFEfdVRVPFLIRGPGIQA- 362
Cdd:cd16024 168 LMPPKLKEMDDV---IKRIYESLEEQSSNNPTLLVVCGDHGMtdagnH--------GGSSPGE--TSVPLLFISPKFSSk 234
|
90 100 110
....*....|....*....|....*....|..
gi 442619385 363 ------SKVVNEIVLNVDLAPTFLDMGGVPTP 388
Cdd:cd16024 235 psnadgELSYYETVQQVDLAPTLALLLGLPIP 266
|
|
| GPI_EPT |
cd16019 |
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in ... |
295-389 |
3.22e-03 |
|
GPI ethanolamine phosphate transferase; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293743 [Multi-domain] Cd Length: 292 Bit Score: 40.81 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 295 QTLQSVDVAVERVYNELKelgelDNTYIVYTSDHG-----YHLGQ---------FGLIKGKSFPFEFDVRVPFLIRGPG- 359
Cdd:cd16019 180 KKLDQMDNLIRDIYDRMD-----NDTLLVVVSDHGmnndgNHGGSsteetssffFFISKKGFFKKRPIDQIEKIKQNNEq 254
|
90 100 110
....*....|....*....|....*....|..
gi 442619385 360 --IQASKVVNEIvLNVDLAPTFLDMGGVPTPQ 389
Cdd:cd16019 255 qkIDPSEYIRII-YQIDILPTICYLLGIPIPF 285
|
|
| GPI_EPT_1 |
cd16020 |
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is ... |
294-398 |
9.60e-03 |
|
GPI ethanolamine phosphate transferase 1; PIG-N; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293744 Cd Length: 294 Bit Score: 39.49 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442619385 294 LQTLQSVDVAVERVYNELKELGELDNTYIVYTSDHG-----YHlgqfglikGKSFPFEfdVRVPFLIRGPGIQASK---- 364
Cdd:cd16020 182 LENIRYVDKGIEKTYPLIEEYFNDGRTAYIFTSDHGmtdwgSH--------GDGSPDE--TETPFIAWGAGIKHPTpgrg 251
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 442619385 365 ---VVNEIVLNV--------DLAP---TFLdmgGVPTPqhMDGRSILP 398
Cdd:cd16020 252 psfSANWGGLRLprhdldqaDLAPlmsALL---GLPPP--VNSVGILP 294
|
|
| |
