|
Name |
Accession |
Description |
Interval |
E-value |
| G6S |
cd16147 |
glucosamine (N-acetyl)-6-sulfatase(G6S, GNS) AND sulfatase 1(SULF1); ... |
34-480 |
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: 593.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGGMTPMKKTRELIGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAAWQKTA 113
Cdd:cd16147 3 NIVLILTDDQDVELGSMDPMPKTKKLLADQGTTFTNAFVTTPLCCPSRASILTGQYAHNHGVTNNSPPGGGYPKFWQNGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 114 EPFAFPVYLNKMRYQTFYCGKYLNQYGSKdaGGVAHVPPGWDQWHALVGNSKYYNYTLSvNGKEEKHGDSYEKDYLTDLV 193
Cdd:cd16147 83 ERSTLPVWLQEAGYRTAYAGKYLNGYGVP--GGVSYVPPGWDEWDGLVGNSTYYNYTLS-NGGNGKHGVSYPGDYLTDVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 194 LNRSLHFLEERSPSH-PFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPR--NGSFNKPGTDKHWLLRQPanPMPNSSIDYL 270
Cdd:cd16147 160 ANKALDFLRRAAADDkPFFLVVAPPAPHGPFTPAPRYANLFPNVTAPPrpPPNNPDVSDKPHWLRRLP--PLNPTQIAYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 271 DNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPGIKAKQTL 350
Cdd:cd16147 238 DELYRKRLRTLQSVDDLVERLVNTLEATGQLDNTYIIYTSDNGYHLGQHRLPPGKRTPYEEDIRVPLLVRGPGIPAGVTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 351 QSPVLNIDLPMTILDIAGVNLSTVnMDGQSflpqmapslrngterpfflveytgegyssqdpscpklgpglaecfpdcvC 430
Cdd:cd16147 318 DQLVSNIDLAPTILDLAGAPPPSD-MDGRS-------------------------------------------------C 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1000814517 431 EDAFNNTYACVRTLKGA-NLQYCEFADNeaFVEMYNLTADPHQLENIVKKV 480
Cdd:cd16147 348 GDSNNNTYKCVRTVDDTyNLLYFEWCTG--FRELYDLTTDPYQLTNLAGDL 396
|
|
| G6S_like |
cd16031 |
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ... |
34-495 |
5.56e-85 |
|
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: 268.63 E-value: 5.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQ-MGGMT-PMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsvEGNcSSAAW 109
Cdd:cd16031 4 NIIFILTDDHRYDaLGCYGnPIVKTPNIdrLAKEGVRFDNAFVTTSICAPSRASILTGQYSHRHGVTDN--NGP-LFDAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 110 QKTaepfaFPVYLNKMRYQTFYCGKYLNQygskdaGGVAHVPPGWDQWHALVGNSKYYNYTLSVNGKEEKhgdsyEKDYL 189
Cdd:cd16031 81 QPT-----YPKLLRKAGYQTAFIGKWHLG------SGGDLPPPGFDYWVSFPGQGSYYDPEFIENGKRVG-----QKGYV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 190 TDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSFNkpgtDKHWLLR-QPANPMPNSSID 268
Cdd:cd16031 145 TDIITDKALDFLKERDKDKPFCLSLSFKAPHRPFTPAPRHRGLYEDVTIPEPETFD----DDDYAGRpEWAREQRNRIRG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 269 YLDNAFRRRW----------QTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLL 338
Cdd:cd16031 221 VLDGRFDTPEkyqrymkdylRTVTGVDDNVGRILDYLEEQGLADNTIIIYTSDNGFFLGEHGL-FDKRLMYEESIRVPLI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 339 VRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQmapsLRNGTERPF---FLVEYTGEGyssqdpsc 414
Cdd:cd16031 300 IRDPRlIKAGTVVDALVLNIDFAPTILDLAGVPIPE-DMQGRSLLPL----LEGEKPVDWrkeFYYEYYEEP-------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 415 pklgpglaecfpdcvcedAFNNTYAC--VRTLKGANLQYCEFADNEafvEMYNLTADPHQLENIVKkvDP---SLLQIMN 489
Cdd:cd16031 367 ------------------NFHNVPTHegVRTERYKYIYYYGVWDEE---ELYDLKKDPLELNNLAN--DPeyaEVLKELR 423
|
....*.
gi 1000814517 490 QRLIKL 495
Cdd:cd16031 424 KRLEEL 429
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
34-502 |
5.27e-78 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 249.41 E-value: 5.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQD-EQMG--GMTPMKkTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAA 108
Cdd:COG3119 25 NILFILADDLGyGDLGcyGNPLIK-TPNIdrLAAEGVRFTNAYVTSPVCSPSRASLLTGRYPHRTGVTDNGEGYNGGLPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 WQKTaepfaFPVYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqWHAlvgnskyynytlsvngkeekhgdsyekdY 188
Cdd:COG3119 104 DEPT-----LAELLKEAGYRTALFGK----------------------WHL----------------------------Y 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 189 LTDLVLNRSLHFLEERS-PSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRngsfnkpgtdkhwllrqPANPMP-NSS 266
Cdd:COG3119 129 LTDLLTDKAIDFLERQAdKDKPFFLYLAFNAPHAPYQAPEEYLDKYDGKDIPL-----------------PPNLAPrDLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 267 IDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IK 345
Cdd:COG3119 192 EEELRRARAAYAAMIEEVDDQVGRLLDALEELGLADNTIVVFTSDNGPSLGEHGLRGGKGTLYEGGIRVPLIVRWPGkIK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 346 AKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQmapsLRNGTE--RPFFLVEYTGEGyssqdpscpklgpglae 423
Cdd:COG3119 272 AGSVSDALVSLIDLLPTLLDLAGVPIPE-DLDGRSLLPL----LTGEKAewRDYLYWEYPRGG----------------- 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1000814517 424 cfpdcvcedafnnTYACVRTlkgANLQYCEFADNEAFVEMYNLTADPHQLENIVKKvDPSLLQIMNQRLIKLQSCAGDT 502
Cdd:COG3119 330 -------------GNRAIRT---GRWKLIRYYDDDGPWELYDLKNDPGETNNLAAD-YPEVVAELRALLEAWLKELGDP 391
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
34-490 |
4.74e-53 |
|
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: 183.48 E-value: 4.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGG-MTPMKKT-------REligdaGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGnCS 105
Cdd:cd16027 2 NILWIIADDLSPDLGGyGGNVVKTpnldrlaAE-----GVRFTNAFTTAPVCSPSRSALLTGLYPHQNGAHGLRSRG-FP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 106 SAAWQKTaepfaFPVYLNKMRYQTFYCGKYlnqygskdaggvaHVPPGWDqwhalvgnskyYNYTLSVNGKEEKHGDSYE 185
Cdd:cd16027 76 LPDGVKT-----LPELLREAGYYTGLIGKT-------------HYNPDAV-----------FPFDDEMRGPDDGGRNAWD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 186 KDYLTDlvlnrslHFLEERSPSHPFFMMLCPPAPHSPWTAAPQYSGSF--SGVKAPRNGsFNKPGTDKHWLlrqpanpmp 263
Cdd:cd16027 127 YASNAA-------DFLNRAKKGQPFFLWFGFHDPHRPYPPGDGEEPGYdpEKVKVPPYL-PDTPEVREDLA--------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 264 nssiDYLDNAFRrrwqtllsVDDLVERLLKKLDSVKELDNTYIFYTSDHGYhtgqfSLPIDKRQLYEFDIRIPLLVRGPG 343
Cdd:cd16027 190 ----DYYDEIER--------LDQQVGEILDELEEDGLLDNTIVIFTSDHGM-----PFPRAKGTLYDSGLRVPLIVRWPG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 344 -IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQMAPSlrNGTERPFFlveytgegYSSQdpscpklgpgla 422
Cdd:cd16027 253 kIKPGSVSDALVSFIDLAPTLLDLAGIEPPE-YLQGRSFLPLLKGE--KDPGRDYV--------FAER------------ 309
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1000814517 423 ecfpdcvceDAFNNTYACVRTLKGANLQYCEfadNEAFVEMYNLTADPHQLENIVKkvDPSLLQIMNQ 490
Cdd:cd16027 310 ---------DRHDETYDPIRSVRTGRYKYIR---NYMPEELYDLKNDPDELNNLAD--DPEYAEVLEE 363
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
34-380 |
5.17e-52 |
|
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: 176.47 E-value: 5.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGGMTPMK--KTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsVEGNCSSAAW 109
Cdd:cd16022 2 NILLIMTDDLGYDDLGCYGNPdiKTPNLdrLAAEGVRFTNAYVASPVCSPSRASLLTGRYPHRHGVRGN-VGNGGGLPPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 110 QKTaepfaFPVYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqWHalvgnskyynytlsvngkeekhgdsyekdyl 189
Cdd:cd16022 81 EPT-----LAELLKEAGYRTALIGK----------------------WH------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 190 tdlvlNRSLHFLEERSPSHPFFMMLCPPAPHSPWTaapqYSGsfsgvkaprngsfnkpgtdkhwllrqpanpmpnssidy 269
Cdd:cd16022 103 -----DEAIDFIERRDKDKPFFLYVSFNAPHPPFA----YYA-------------------------------------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 270 ldnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFDIRIPLLVRGPG-IKAKQ 348
Cdd:cd16022 136 ----------MVSAIDDQIGRILDALEELGLLDNTLIVFTSDHGDMLGDHGLRGKKGSLYEGGIRVPFIVRWPGkIPAGQ 205
|
330 340 350
....*....|....*....|....*....|..
gi 1000814517 349 TLQSPVLNIDLPMTILDIAGVNLSTvNMDGQS 380
Cdd:cd16022 206 VSDALVSLLDLLPTLLDLAGIEPPE-GLDGRS 236
|
|
| Sulfatase |
pfam00884 |
Sulfatase; |
34-369 |
8.71e-50 |
|
Sulfatase;
Pssm-ID: 459979 [Multi-domain] Cd Length: 298 Bit Score: 172.61 E-value: 8.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQ-DEQMG--GMtPMKKTRELIGDA--GATFSNAFTSTPLCCPSRSSFLSGRYPHNHlvhnnsveGNCSSAA 108
Cdd:pfam00884 2 NVVLVLGESLrAPDLGlyGY-PRPTTPFLDRLAeeGLLFSNFYSGGTLTAPSRFALLTGLPPHNF--------GSYVSTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 WQKTAEPFAFPVYLNKMRYQTFYCGKYLNQYGSKDAGGV--AHVPPGWDQWHALVGNSKYYNYTLSVNGkeekhgdsyek 186
Cdd:pfam00884 73 VGLPRTEPSLPDLLKRAGYNTGAIGKWHLGWYNNQSPCNlgFDKFFGRNTGSDLYADPPDVPYNCSGGG----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 187 dYLTDLVLNRSLHFLeeRSPSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAprngsfnkpgtdkhwllrqpanpmpnsS 266
Cdd:pfam00884 142 -VSDEALLDEALEFL--DNNDKPFFLVLHTLGSHGPPYYPDRYPEKYATFKP---------------------------S 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 267 IDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPID---KRQLYEFDIRIPLLVRGPG 343
Cdd:pfam00884 192 SCSEEQLLNSYDNTLLYTDDAIGRVLDKLEENGLLDNTLVVYTSDHGESLGEGGGYLHggkYDNAPEGGYRVPLLIWSPG 271
|
330 340
....*....|....*....|....*..
gi 1000814517 344 IKAKQTLQSPVLN-IDLPMTILDIAGV 369
Cdd:pfam00884 272 GKAKGQKSEALVShVDLFPTILDLAGI 298
|
|
| sulfatase_like |
cd16033 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
33-492 |
3.30e-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: 293757 [Multi-domain] Cd Length: 411 Bit Score: 171.63 E-value: 3.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 33 NNIILILTDDQ--DEQMGGMTPMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAA 108
Cdd:cd16033 1 PNILFIMTDQQryDTLGCYGNPIVKTPNIdrLAAEGVRFTNAYTPSPVCCPARASLLTGLYPHEHGVLNNVENAGAYSRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 WQKTAEpfAFPVYLNKMRYQTFYCGKY--LNQYGSKDAGGVAHVPpgwdqwhalvgnskyynytlsvngkEEKHGDSYek 186
Cdd:cd16033 81 LPPGVE--TFSEDLREAGYRNGYVGKWhvGPEETPLDYGFDEYLP-------------------------VETTIEYF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 187 dyLTDLVLNRSLHFLEErspSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSFNKPGTDKHWLLRQPANpMPNss 266
Cdd:cd16033 132 --LADRAIEMLEELAAD---DKPFFLRVNFWGPHDPYIPPEPYLDMYDPEDIPLPESFADDFEDKPYIYRRERK-RWG-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 267 idyLDNAFRRRWQTLLS--------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQ-LYEFDIRIPL 337
Cdd:cd16033 204 ---VDTEDEEDWKEIIAhywgyitlIDDAIGRILDALEELGLADDTLVIFTSDHGDALGAHRL-WDKGPfMYEETYRIPL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 338 LVRGPGIKAK-QTLQSPVLNIDLPMTILDIAGVnLSTVNMDGQSFLPQmapsLRNGTERPF---FLVEYTGEGYssqdps 413
Cdd:cd16033 280 IIKWPGVIAAgQVVDEFVSLLDLAPTILDLAGV-DVPPKVDGRSLLPL----LRGEQPEDWrdeVVTEYNGHEF------ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 414 cpklgpglaecfpdcvcedafnntYACVRTLKGANLQYCEfaDNEAFVEMYNLTADPHQLENIVK-KVDPSLLQIMNQRL 492
Cdd:cd16033 349 ------------------------YLPQRMVRTDRYKYVF--NGFDIDELYDLESDPYELNNLIDdPEYEEILREMRTRL 402
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-476 |
1.44e-47 |
|
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: 169.67 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDdqdeQMGGMT------PMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHlvhnnSVEGN 103
Cdd:cd16034 1 KPNILFIFAD----QHRAQAlgcagdDPVKTPNLdrLAKEGVVFTNAVSNYPVCSPYRASLLTGQYPLTN-----GVFGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 104 CSSaaWQKTAEPFAfpVYLNKMRYQTFYCGKY-LNQYGSKDAGGVAHVPP-----GWDQWHALVGNSKYYNYTLSVNGKE 177
Cdd:cd16034 72 DVP--LPPDAPTIA--DVLKDAGYRTGYIGKWhLDGPERNDGRADDYTPPperrhGFDYWKGYECNHDHNNPHYYDDDGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 178 EKHGDSYEKDYLTDLVLNrslhFLEERS-PSHPFFMMLCPPAPHSPWTAAPQ-YSGSFSgvkaprngsfnkpgtDKHWLL 255
Cdd:cd16034 148 RIYIKGYSPDAETDLAIE----YLENQAdKDKPFALVLSWNPPHDPYTTAPEeYLDMYD---------------PKKLLL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 256 RqpanpmPNSSIDYLDNAFRRRWQT-----LLSVDDLVERLLKKLDSVKELDNTYIFYTSDHG---YHTGQFSlpidKRQ 327
Cdd:cd16034 209 R------PNVPEDKKEEAGLREDLRgyyamITALDDNIGRLLDALKELGLLENTIVVFTSDHGdmlGSHGLMN----KQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 328 LYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFlpqmAPSLRNGTERPFFLVEY---- 402
Cdd:cd16034 279 PYEESIRVPFIIRYPGkIKAGRVVDLLINTVDIMPTLLGLCGLPIPD-TVEGRDL----SPLLLGGKDDEPDSVLLqcfv 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1000814517 403 -TGEGYSSQDPscpklgpglaecfpdcvcedafnnTYACVRTLKGanlQYCEFADNEAFveMYNLTADPHQLENI 476
Cdd:cd16034 354 pFGGGSARDGG------------------------EWRGVRTDRY---TYVRDKNGPWL--LFDNEKDPYQLNNL 399
|
|
| ARS_like |
cd16144 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
34-398 |
3.26e-46 |
|
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: 166.56 E-value: 3.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMGGM-----------TP-MkktreligDA----GATFSNAFTSTPLCCPSRSSFLSGRYP------H 91
Cdd:cd16144 2 NIVLILVDD----LGWAdlgcygskfyeTPnI--------DRlakeGMRFTQAYAAAPVCSPSRASILTGQYParlgitD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 92 NHLVHNNSVEGNCSSAAWQKT---AEPFAFPVYLNKMRYQTFYCGKY----LNQYGSKDAG---GVAHvppgwDQWHAlv 161
Cdd:cd16144 70 VIPGRRGPPDNTKLIPPPSTTrlpLEEVTIAEALKDAGYATAHFGKWhlggEGGYGPEDQGfdvNIGG-----TGNGG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 162 GNSKYYNYTLSVNGKEEKhgdsYEKDYLTDLVLNRSLHFLEERSpSHPFFMMLCPPAPHSPWTAapqysgsfsgvkaprn 241
Cdd:cd16144 143 PPSYYFPPGKPNPDLEDG----PEGEYLTDRLTDEAIDFIEQNK-DKPFFLYLSHYAVHTPIQA---------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 242 gsfnKPGTDKHWLLRQPANPMPNSSIDYLdnafrrrwqTLL-SVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFS 320
Cdd:cd16144 202 ----RPELIEKYEKKKKGLRKGQKNPVYA---------AMIeSLDESVGRILDALEELGLADNTLVIFTSDNGGLSTRGG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 321 LPID-------KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTV-NMDGQSFLPQMAPSLRN 391
Cdd:cd16144 269 PPTSnaplrggKGSLYEGGIRVPLIVRWPGvIKPGSVSDVPVIGTDLYPTFLELAGGPLPPPqHLDGVSLVPLLKGGEAD 348
|
....*..
gi 1000814517 392 GTERPFF 398
Cdd:cd16144 349 LPRRALF 355
|
|
| sulfatase_like |
cd16152 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-495 |
1.92e-38 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293771 [Multi-domain] Cd Length: 373 Bit Score: 144.29 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDDQD-EQMGGM-TPMKKTRELIGDA--GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVegncSSA 107
Cdd:cd16152 1 KPNVIVFFTDQQRwDTLGCYgQPLDLTPNLDALAeeGVLFENAFTPQPVCGPARACLQTGLYPTETGCFRNGI----PLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 108 AWQKT-AEpfafpvYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqWHaLVGnskyynytlsvngkeekhgdsYEK 186
Cdd:cd16152 77 ADEKTlAH------YFRDAGYETGYVGK----------------------WH-LAG---------------------YRV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 187 DYLTDLVLNrslhFLEERSPSHPFFMML------------CPPAPHspwtaapqysGSfsgvkAPRNGSFNKPGtDkhwL 254
Cdd:cd16152 107 DALTDFAID----YLDNRQKDKPFFLFLsylephhqndrdRYVAPE----------GS-----AERFANFWVPP-D---L 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 255 LRQPANP---MPnssiDYLdNAFRRrwqtllsVDDLVERLLKKLDSVKELDNTYIFYTSDHGYH----TGQFslpidKRQ 327
Cdd:cd16152 164 AALPGDWaeeLP----DYL-GCCER-------LDENVGRIRDALKELGLYDNTIIVFTSDHGCHfrtrNAEY-----KRS 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 328 LYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLStVNMDGQSFLPQMAPSLRNGTERPFFLVEYTGEG- 406
Cdd:cd16152 227 CHESSIRVPLVIYGPGFNGGGRVEELVSLIDLPPTLLDAAGIDVP-EEMQGRSLLPLVDGKVEDWRNEVFIQISESQVGr 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 407 --------YSSQDpscPKLGPGlaecfpdcvcEDAFNNTYAcvrtlkganlqycefadnEAFveMYNLTADPHQLENIVK 478
Cdd:cd16152 306 airtdrwkYSVAA---PDKDGW----------KDSGSDVYV------------------EDY--LYDLEADPYELVNLIG 352
|
490 500
....*....|....*....|
gi 1000814517 479 kvDPSLLQI---MNQRLIKL 495
Cdd:cd16152 353 --RPEYREVaaeLRERLLAR 370
|
|
| ARS_like |
cd16146 |
uncharacterized arylsulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide ... |
34-398 |
7.92e-38 |
|
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: 143.46 E-value: 7.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQ---DEQMGGmTPMKKTREL--IGDAGATFSNaFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNcssaa 108
Cdd:cd16146 2 NVILILTDDQgygDLGFHG-NPILKTPNLdrLAAESVRFTN-FHVSPVCAPTRAALLTGRYPFRTGVWHTILGRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 wqktaepfafpvylnKMR--------------YQTFYCGKYLN----QYGSKD----------AGGVAHVPPGWdqwhal 160
Cdd:cd16146 75 ---------------RMRldettlaevfkdagYRTGIFGKWHLgdnyPYRPQDrgfdevlghgGGGIGQYPDYW------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 161 vgNSKYYNYTLSVNGKEEKHgdsyeKDYLTDLVLNRSLHFLEERSpSHPFFMMLCPPAPHSPWTAAPQYSGsfsgvkapr 240
Cdd:cd16146 134 --GNDYFDDTYYHNGKFVKT-----EGYCTDVFFDEAIDFIEENK-DKPFFAYLATNAPHGPLQVPDKYLD--------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 241 ngsfnkpgtdkhwllrqpanpmpnssiDYLDNAFRRRWQTLL----SVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHT 316
Cdd:cd16146 197 ---------------------------PYKDMGLDDKLAAFYgmieNIDDNVGRLLAKLKELGLEENTIVIFMSDNGPAG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 317 GqfslpIDKR----------QLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLS-TVNMDGQSFLPQ 384
Cdd:cd16146 250 G-----VPKRfnagmrgkkgSVYEGGHRVPFFIRWPGkILAGKDVDTLTAHIDLLPTLLDLCGVKLPeGIKLDGRSLLPL 324
|
410
....*....|....
gi 1000814517 385 MAPSLRNGTERPFF 398
Cdd:cd16146 325 LKGESDPWPERTLF 338
|
|
| iduronate-2-sulfatase |
cd16030 |
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the ... |
64-479 |
5.39e-37 |
|
iduronate-2-sulfatase; Iduronate 2-sulfatase is a sulfatase enzyme that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Iduronate 2-sulfatase is required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Mutations in the iduronate 2-sulfatase gene that result in enzymatic deficiency lead to the sex-linked mucopolysaccharidosis type II, also known as Hunter syndrome.
Pssm-ID: 293754 [Multi-domain] Cd Length: 435 Bit Score: 141.56 E-value: 5.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 64 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssAAWQKTAEPFA-FPVYLNKMRYQTFYCGKYLNQYGSK 142
Cdd:cd16030 37 GVLFTNAYCQQPVCGPSRASLLTGRRPDTTGVYDNN-------SYFRKVAPDAVtLPQYFKENGYTTAGVGKIFHPGIPD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 143 DAggvaHVPPGWDQWHALVGNSKYYNYTLSVNGKEEKHG---------DSYEKDYLTDLVLNRSLHFLEERSPSH-PFFM 212
Cdd:cd16030 110 GD----DDPASWDEPPNPPGPEKYPPGKLCPGKKGGKGGgggpaweaaDVPDEAYPDGKVADEAIEQLRKLKDSDkPFFL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 213 mlcppA-----PHSPWTAaPQ-----YSGSfSGVKAPRNGSFNKPGTDKHwllrqPANPMPNSSIDYLDNAFRR------ 276
Cdd:cd16030 186 -----AvgfykPHLPFVA-PKkyfdlYPLE-SIPLPNPFDPIDLPEVAWN-----DLDDLPKYGDIPALNPGDPkgplpd 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 277 -RWQTLLS--------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYH---TGQFSlpidKRQLYEFDIRIPLLVRGPGI 344
Cdd:cd16030 254 eQARELRQayyasvsyVDAQVGRVLDALEELGLADNTIVVLWSDHGWHlgeHGHWG----KHTLFEEATRVPLIIRAPGV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 345 KAK-QTLQSPVLNIDL-PmTILDIAGVNlSTVNMDGQSFLPQMapslrngterpfflveytgegyssQDPSCPKLGPGLA 422
Cdd:cd16030 330 TKPgKVTDALVELVDIyP-TLAELAGLP-APPCLEGKSLVPLL------------------------KNPSAKWKDAAFS 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1000814517 423 EcFPDCVcedafNNTYAcVRTlkgANLQYCEFADNEA--FVEMYNLTADPHQLENIVKK 479
Cdd:cd16030 384 Q-YPRPS-----IMGYS-IRT---ERYRYTEWVDFDKvgAEELYDHKNDPNEWKNLAND 432
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-386 |
1.55e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293760 [Multi-domain] Cd Length: 321 Bit Score: 137.67 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGGMT--PMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssAAW 109
Cdd:cd16037 2 NILIIMSDEHNPDAMGCYghPVVRTPNLdrLAARGTRFENAYTPSPICVPSRASFLTGRYVHETGVWDNA-------DPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 110 QKTAEpfAFPVYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqwhalvgnskyynytLSVNGKEEKHGDSYEKDyl 189
Cdd:cd16037 75 DGDVP--SWGHALRAAGYETVLIGK------------------------------------LHFRGEDQRHGFRYDRD-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 190 tdlVLNRSLHFLEERSPS-HPFFMMLCPPAPHSPWTAAPQysgsfsgvkaprngsfnkpgtdkHWLLrqpanpmpnssid 268
Cdd:cd16037 115 ---VTEAAVDWLREEAADdKPWFLFVGFVAPHFPLIAPQE-----------------------FYDL------------- 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 269 YLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPGIKAKQ 348
Cdd:cd16037 156 YVRRARAAYYGLVEFLDENIGRVLDALEELGLLDNTLIIYTSDHGDMLGERGL-WGKSTMYEESVRVPMIISGPGIPAGK 234
|
330 340 350
....*....|....*....|....*....|....*...
gi 1000814517 349 TLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQMA 386
Cdd:cd16037 235 RVKTPVSLVDLAPTILEAAGAPPPP-DLDGRSLLPLAE 271
|
|
| sulfatase_like |
cd16150 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-494 |
1.64e-36 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293769 [Multi-domain] Cd Length: 423 Bit Score: 140.06 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDdqdeQM-----GGM-TPMKKTRELigDA----GATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvhnnsVEGN 103
Cdd:cd16150 2 NIVIFVAD----QLradslGHLgNPAAVTPNL--DAlaaeGVRFSNAYCQNPVCSPSRCSFLTGWYPH--------VNGH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 104 CSSAAWQKTAEPfafpVYLNKMR---YQTFYCGKylnqygskdaggvAHVPPGWDQWhalvgnskyynytlsvngkeekh 180
Cdd:cd16150 68 RTLHHLLRPDEP----NLLKTLKdagYHVAWAGK-------------NDDLPGEFAA----------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 181 gDSYEKDylTDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNgsfnKPGTDKHwllrqPAN 260
Cdd:cd16150 108 -EAYCDS--DEACVRTAIDWLRNRRPDKPFCLYLPLIFPHPPYGVEEPWFSMIDREKLPPR----RPPGLRA-----KGK 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 261 PM-----PNSSIDYLDNAfrrRWQTLLSV--------DDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpIDKRQ 327
Cdd:cd16150 176 PSmlegiEKQGLDRWSEE---RWRELRATylgmvsrlDHQFGRLLEALKETGLYDDTAVFFFSDHGDYTGDYGL-VEKWP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 328 --LYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLSTVNMdGQSFLPQMAPSLRNGTERPF----FLVE 401
Cdd:cd16150 252 ntFEDCLTRVPLIIKPPGGPAGGVSDALVELVDIPPTLLDLAGIPLSHTHF-GRSLLPVLAGETEEHRDAVFseggRLHG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 402 YTG--EGYSsqDPSCPKLGPGLAECFPDCVCEdAF---NNTYACVRTLKGANlqycefadneafvEMYNLTADPHQLENI 476
Cdd:cd16150 331 EEQamEGGH--GPYDLKWPRLLQQEEPPEHTK-AVmirTRRYKYVYRLYEPD-------------ELYDLEADPLELHNL 394
|
490 500
....*....|....*....|.
gi 1000814517 477 VKkvDP---SLLQIMNQRLIK 494
Cdd:cd16150 395 IG--DPayaEIIAEMKQRLLR 413
|
|
| ARS_like |
cd16143 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
34-477 |
8.14e-34 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293762 [Multi-domain] Cd Length: 395 Bit Score: 131.94 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMGgmtpmkktrelIGD--------------------AGATFSNAFTSTPLCCPSRSSFLSGRYPHNH 93
Cdd:cd16143 2 NIVIILADD----LG-----------YGDiscynpdskiptpnidrlaaEGMRFTDAHSPSSVCTPSRYGLLTGRYPWRS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 94 LVHNNSVEGNCSSA--AWQKTaepfaFPVYLNKMRYQTFYCGKYlnqygskdaggvaHVppGWDqWHALVGNSKYYNYTL 171
Cdd:cd16143 67 RLKGGVLGGFSPPLiePDRVT-----LAKMLKQAGYRTAMVGKW-------------HL--GLD-WKKKDGKKAATGTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 172 SVN-GKEEKHG------DSYekdYLT------DLVLNRSLHFLEERS-PSHPFFMMLCPPAPHSPWTAAPQYSGSfSGvk 237
Cdd:cd16143 126 DVDySKPIKGGpldhgfDYY---FGIpasevlPTLTDKAVEFIDQHAkKDKPFFLYFALPAPHTPIVPSPEFQGK-SG-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 238 aprngsfnkpgtdkhwllrqpANPmpnssidYLDnaFrrrwqtLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHG---Y 314
Cdd:cd16143 200 ---------------------AGP-------YGD--F------VYELDWVVGRILDALKELGLAENTLVIFTSDNGpspY 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 315 HTGQFSLPID----------KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNL-STVNMDGQSFL 382
Cdd:cd16143 244 ADYKELEKFGhdpsgplrgmKADIYEGGHRVPFIVRWPGkIPAGSVSDQLVSLTDLFATLAAIVGQKLpDNAAEDSFSFL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 383 PQMAPslRNGTERPFFLVEYTGEGYSS--QDPScpKLgpglaecfpdCVCEDAFNNTYACVRTLKGANlqycefadneaF 460
Cdd:cd16143 324 PALLG--PKKQEVRESLVHHSGNGSFAirKGDW--KL----------IDGTGSGGFSYPRGKEKLGLP-----------P 378
|
490
....*....|....*..
gi 1000814517 461 VEMYNLTADPHQLENIV 477
Cdd:cd16143 379 GQLYNLSTDPGESNNLY 395
|
|
| sulfatase_like |
cd16156 |
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ... |
34-403 |
1.37e-32 |
|
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: 129.81 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGGM---TPMKkTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNhlvhnNSVEGNCSSAA 108
Cdd:cd16156 2 QFIFIMTDTQRWDMVGCygnKAMK-TPNLdrLAAEGVRFDSAYTTQPVCGPARSGLFTGLYPHT-----NGSWTNCMALG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 WQ-KTaepfaFPVYLNKMRYQTFYCGKYLNQYGskDAGGVAHVPPGWDQ--WHALVgnskyyNY---------TLSVNGK 176
Cdd:cd16156 76 DNvKT-----IGQRLSDNGIHTAYIGKWHLDGG--DYFGNGICPQGWDPdyWYDMR------NYldelteeerRKSRRGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 177 EEKHGDSYEKDY-LTDLVLNRSLHFLEERSpSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSF-----NKPGTD 250
Cdd:cd16156 143 TSLEAEGIKEEFtYGHRCTNRALDFIEKHK-DEDFFLVVSYDEPHHPFLCPKPYASMYKDFEFPKGENAyddleNKPLHQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 251 KHWllrqpANPMPNSSIDYLD---------NAFrrrwqtllsVDDLVERLLKKLDsvKELDNTYIFYTSDHGYHTGQFSL 321
Cdd:cd16156 222 RLW-----AGAKPHEDGDKGTikhplyfgcNSF---------VDYEIGRVLDAAD--EIAEDAWVIYTSDHGDMLGAHKL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 322 PIDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTVnMDGQSFLPQMAPslRNGTERPFFLV 400
Cdd:cd16156 286 WAKGPAVYDEITNIPLIIRGKGgEKAGTVTDTPVSHIDLAPTILDYAGIPQPKV-LEGESILATIED--PEIPENRGVFV 362
|
...
gi 1000814517 401 EYT 403
Cdd:cd16156 363 EFG 365
|
|
| choline-sulfatase |
cd16032 |
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ... |
34-409 |
1.40e-32 |
|
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: 126.92 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDdqdeQMGG-MTPMK-----KTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvhnnsvegncS 105
Cdd:cd16032 2 NILLIMAD----QLTAaALPAYgntvvKTPNLdrLAARGVVFDNAYCNSPLCAPSRASMMTGRLPS-------------R 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 106 SAAWQKTAEpFA-----FPVYLNKMRYQTFYCGKylnqygskdaggvAH-VPPgwDQwhalvgnskyynytlsvngkeeK 179
Cdd:cd16032 65 IGAYDNAAE-FPadiptFAHYLRAAGYRTALSGK-------------MHfVGP--DQ----------------------L 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 180 HGDSYEkdyltDLVLNRSLHFLEERSPSH---PFFMMLCPPAPHSPWTAAPQYsgsfsgvkaprngsfnkpgtdkhWLLr 256
Cdd:cd16032 107 HGFDYD-----EEVAFKAVQKLYDLARGEdgrPFFLTVSFTHPHDPYVIPQEY-----------------------WDL- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 257 qpanpmpnssidYLDNAfRRRWQTLLS-VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIdKRQLYEFDIRI 335
Cdd:cd16032 158 ------------YVRRA-RRAYYGMVSyVDDKVGQLLDTLERTGLADDTIVIFTSDHGDMLGERGLWY-KMSFFEGSARV 223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1000814517 336 PLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLSTVN--MDGQSFLPQMApSLRNGTERPFFlVEYTGEGYSS 409
Cdd:cd16032 224 PLIISAPGRFAPRRVAEPVSLVDLLPTLVDLAGGGTAPHVppLDGRSLLPLLE-GGDSGGEDEVI-SEYLAEGAVA 297
|
|
| ARS_like |
cd16145 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
34-406 |
1.79e-32 |
|
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293764 [Multi-domain] Cd Length: 415 Bit Score: 128.48 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMG-GMT-----PMKKTRELigDA----GATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHNNSVEG 102
Cdd:cd16145 2 NIIFILADD----LGyGDLgcygqKKIKTPNL--DRlaaeGMRFTQHYAGAPVCAPSRASLLTGLHTgHTRVRGNSEPGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 103 ncssaAWQKTAEPFAFPVYLNKMRYQTFYCGKylnqYGSKDAGGVAHVPP-GWDQW-------HA-------LVGNSKY- 166
Cdd:cd16145 76 -----QDPLPPDDVTLAEVLKKAGYATAAFGK----WGLGGPGTPGHPTKqGFDYFygyldqvHAhnyypeyLWRNGEKv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 167 -YNYTLSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEERSpSHPFFMMLCPPAPHSPWtAAPQYSGSFsgvkaprnGSFN 245
Cdd:cd16145 147 pLPNNVIPPLDEGNNAGGGGGTYSHDLFTDEALDFIRENK-DKPFFLYLAYTLPHAPL-QVPDDGPYK--------YKPK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 246 KPGTDKHWLLRQPanpmpnssidyldnafRRRWQTLLS-VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHT-GQFSLPI 323
Cdd:cd16145 217 DPGIYAYLPWPQP----------------EKAYAAMVTrLDRDVGRILALLKELGIDENTLVVFTSDNGPHSeGGSEHDP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 324 D-----------KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTvNMDGQSFLPQMAPSLRN 391
Cdd:cd16145 281 DffdsngplrgyKRSLYEGGIRVPFIARWPGkIPAGSVSDHPSAFWDFMPTLADLAGAEPPE-DIDGISLLPTLLGKPQQ 359
|
410
....*....|....*
gi 1000814517 392 GTERPFFLVEYTGEG 406
Cdd:cd16145 360 QQHDYLYWEFYEGGG 374
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
31-383 |
7.92e-32 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293774 [Multi-domain] Cd Length: 372 Bit Score: 125.75 E-value: 7.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 31 SKNNIILILTDDQD-EQMGGM------TP-MKKtreLIgDAGATFSNAF----TSTPLCCPSRSSFLSGRYphnhlVHNN 98
Cdd:cd16155 1 KKPNILFILADDQRaDTIGALgnpeiqTPnLDR---LA-RRGTSFTNAYnmggWSGAVCVPSRAMLMTGRT-----LFHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 99 SVEGNCSSAAWQKTaepfaFPVYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqWHalvgnskyynytlsvNGkee 178
Cdd:cd16155 72 PEGGKAAIPSDDKT-----WPETFKKAGYRTFATGK----------------------WH---------------NG--- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 179 kHGDSYEKdyltdlvlnrslhFLEERSPS-HPFFMMLCPPAPHSPWTAAPQYSGSFSGVKAPRNGSFnkpgtdkhwllrQ 257
Cdd:cd16155 107 -FADAAIE-------------FLEEYKDGdKPFFMYVAFTAPHDPRQAPPEYLDMYPPETIPLPENF------------L 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 258 PANPMPNSSI---DYLDNAFRRRWQTLLS-----------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpI 323
Cdd:cd16155 161 PQHPFDNGEGtvrDEQLAPFPRTPEAVRQhlaeyyamithLDAQIGRILDALEASGELDNTIIVFTSDHGLAVGSHGL-M 239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000814517 324 DKRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNL-STVnmDGQSFLP 383
Cdd:cd16155 240 GKQNLYEHSMRVPLIISGPGIPKGKRRDALVYLQDVFPTLCELAGIEIpESV--EGKSLLP 298
|
|
| sulfatase_like |
cd16149 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-383 |
4.81e-30 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293768 [Multi-domain] Cd Length: 257 Bit Score: 118.11 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDE-QMGG-MTPMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVEGNCSSAaw 109
Cdd:cd16149 2 NILFILTDDQGPwALGCyGNSEAVTPNLdrLAAEGVRFENFFCTSPVCSPARASLLTGRMPSQHGIHDWIVEGSHGKT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 110 qKTAEPF-----AFPVYLNKMRYQTFYCGKylnqygskdaggvahvppgwdqWHalVGnskyynytlsvngkeekhgdsy 184
Cdd:cd16149 80 -KKPEGYlegqtTLPEVLQDAGYRCGLSGK----------------------WH--LG---------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 185 ekDYLTDlvlnrslHFLEERSPSHPFFMMLCPPAPHSPWtaapQYSGSFSGVkaprngsfnkpgtdkhwllrqpanpmpn 264
Cdd:cd16149 113 --DDAAD-------FLRRRAEAEKPFFLSVNYTAPHSPW----GYFAAVTGV---------------------------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 265 ssidyldnafrrrwqtllsvDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSL--------PIDkrqLYEFDIRIP 336
Cdd:cd16149 152 --------------------DRNVGRLLDELEELGLTENTLVIFTSDNGFNMGHHGIwgkgngtfPLN---MYDNSVKVP 208
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1000814517 337 LLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLST-VNMDGQSFLP 383
Cdd:cd16149 209 FIIRWPGvVPAGRVVDSLVSAYDFFPTLLELAGVDPPAdPRLPGRSFAD 257
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
33-383 |
5.62e-30 |
|
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: 121.98 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 33 NNIILIlTDDQ---DEQMGGMTPMKKTRELigDA----GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSVegncs 105
Cdd:cd16028 1 RNVLFI-TADQwraDCLSCLGHPLVKTPNL--DRlaaeGVRFRNHYTQAAPCGPSRASLYTGRYLMNHRSVWNGT----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 106 saawqktaePFA-----FPVYLNKMRYQTfycgkYLNQYG--SKDAGGVAHV-PPGWDQWHALVGnskyYNYTLSVNGKE 177
Cdd:cd16028 73 ---------PLDarhltLALELRKAGYDP-----ALFGYTdtSPDPRGLAPLdPRLLSYELAMPG----FDPVDRLDEYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 178 EKHGDSyekDYLTDlvlnRSLHFLEERsPSHPFFMMLCPPAPHSPWTAAPQYSGSF--SGVKAP-RNGSFNKPGTD---- 250
Cdd:cd16028 135 AEDSDT---AFLTD----RAIEYLDER-QDEPWFLHLSYIRPHPPFVAPAPYHALYdpADVPPPiRAESLAAEAAQhpll 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 251 KHWLLRQPANP--MPNSSIDYLDNAFRRRWQT----LLS-VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLpI 323
Cdd:cd16028 207 AAFLERIESLSfsPGAANAADLDDEEVAQMRAtylgLIAeVDDHLGRLFDYLKETGQWDDTLIVFTSDHGEQLGDHWL-W 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000814517 324 DKRQLYEFDIRIPLLVRGPGIKAKQTLQS----PVLNIDLPMTILDIAGVNLSTVnMDGQSFLP 383
Cdd:cd16028 286 GKDGFFDQAYRVPLIVRDPRREADATRGQvvdaFTESVDVMPTILDWLGGEIPHQ-CDGRSLLP 348
|
|
| PAS_like |
cd16025 |
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins; Sulfatases catalyze ... |
34-396 |
4.42e-29 |
|
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: 118.70 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMG----GM------TPmkkTRELIGDAGATFSNaFTSTPLCCPSRSSFLSGRYphNHLVHNNSVegn 103
Cdd:cd16025 4 NILLILADD----LGfsdlGCfggeipTP---NLDALAAEGLRFTN-FHTTALCSPTRAALLTGRN--HHQVGMGTM--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 104 cssaawqkTAEPFAFPVY---LNK--------MR---YQTFYCGKylnqygskdaggvahvppgwdqWHalVGNSKYYny 169
Cdd:cd16025 71 --------AELATGKPGYegyLPDsaatiaevLKdagYHTYMSGK----------------------WH--LGPDDYY-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 170 tLSvngkeekhgdsyekDYLTDlvlnRSLHFLEE-RSPSHPFFMMLCPPAPHSPWTAAPQYSGSFSGVkaprngsFNKpG 248
Cdd:cd16025 117 -ST--------------DDLTD----KAIEYIDEqKAPDKPFFLYLAFGAPHAPLQAPKEWIDKYKGK-------YDA-G 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 249 TDKhwlLRQ------------PAN----PMPNSSIDY--LDNAfRRRWQTLL---------SVDDLVERLLKKLDSVKEL 301
Cdd:cd16025 170 WDA---LREerlerqkelgliPADtkltPRPPGVPAWdsLSPE-EKKLEARRmevyaamveHMDQQIGRLIDYLKELGEL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 302 DNTYIFYTSDHG--YHTG--QFS---LPIDKRQLYEFDIRIPLLVRGP-GIKAKQTLQS-PVLNIDLPMTILDIAGVNL- 371
Cdd:cd16025 246 DNTLIIFLSDNGasAEPGwaNASntpFRLYKQASHEGGIRTPLIVSWPkGIKAKGGIRHqFAHVIDIAPTILELAGVEYp 325
|
410 420 430
....*....|....*....|....*....|.
gi 1000814517 372 STVN------MDGQSflpqMAPSLRNGTERP 396
Cdd:cd16025 326 KTVNgvpqlpLDGVS----LLPTLDGAAAPS 352
|
|
| sulfatase_like |
cd16151 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-385 |
1.10e-28 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293770 [Multi-domain] Cd Length: 377 Bit Score: 116.93 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMGgmtpmkktRELIGDAGAT----------------FSNAFtSTPLCCPSRSSFLSGRYPHNHLVHN 97
Cdd:cd16151 2 NIILIMADD----LG--------YECIGCYGGEsyktpnidalaaegvrFNNAY-AQPLCTPSRVQLMTGKYNFRNYVVF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 98 NSVEGNcssaawQKTaepfaFPVYLNKMRYQTFYCGKY--LNQYGSKDAggVAHVppGWDQ---WHALVGNSKYYNYTLS 172
Cdd:cd16151 69 GYLDPK------QKT-----FGHLLKDAGYATAIAGKWqlGGGRGDGDY--PHEF--GFDEyclWQLTETGEKYSRPATP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 173 VNGKEEKHGDSYEK-DYLTDLVLNRSLHFLeERSPSHPFF----MMLcppaPHSPWTAAPQysgsfSGVKAP-RNGSFNK 246
Cdd:cd16151 134 TFNIRNGKLLETTEgDYGPDLFADFLIDFI-ERNKDQPFFayypMVL----VHDPFVPTPD-----SPDWDPdDKRKKDD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 247 PGTDKHwllrqpanpMpnssIDYLdnafrrrwqtllsvDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPID-- 324
Cdd:cd16151 204 PEYFPD---------M----VAYM--------------DKLVGKLVDKLEELGLRENTIIIFTGDNGTHRPITSRTNGre 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000814517 325 ----KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNL-STVNMDGQSFLPQM 385
Cdd:cd16151 257 vrggKGKTTDAGTHVPLIVNWPGlIPAGGVSDDLVDFSDFLPTLAELAGAPLpEDYPLDGRSFAPQL 323
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
64-383 |
6.44e-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: 293767 [Multi-domain] Cd Length: 271 Bit Score: 109.56 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 64 GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNnsvegncssaaWQKTAEPFAFPVYLNKMRYQTFYCGkylnqygskD 143
Cdd:cd16148 36 GVVFDNHYSGSNPTLPSRFSLFTGLYPFYHGVWG-----------GPLEPDDPTLAEILRKAGYYTAAVS---------S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 144 AGGVaHVPPGWDQwhalvgnskYYNYTLSVNGKEEKHGDsyEKDYLTDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSPW 223
Cdd:cd16148 96 NPHL-FGGPGFDR---------GFDTFEDFRGQEGDPGE--EGDERAERVTDRALEWLDRNADDDPFFLFLHYFDPHEPY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 224 taapQYSGSfsgvkaprngsfnkpgtdkhwlLRQpanpmpnssidyldnafrrrwqtllsVDDLVERLLKKLDSVKELDN 303
Cdd:cd16148 164 ----LYDAE----------------------VRY--------------------------VDEQIGRLLDKLKELGLLED 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 304 TYIFYTSDHG--------YHTGQFSLpidkrqlYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLSTVn 375
Cdd:cd16148 192 TLVIVTSDHGeefgehglYWGHGSNL-------YDEQLHVPLIIRWPGKEPGKRVDALVSHIDIAPTLLDLLGVEPPDY- 263
|
....*...
gi 1000814517 376 MDGQSFLP 383
Cdd:cd16148 264 SDGRSLLP 271
|
|
| sulfatase_like |
cd16154 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-383 |
6.34e-25 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293773 [Multi-domain] Cd Length: 372 Bit Score: 105.89 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQ----DEQMGGMTPMKKTREL--IGDAGATFSNAFtSTPLCCPSRSSFLSGRYPHNHLVhnNSVEGNCSSa 107
Cdd:cd16154 2 NILLIIADDQgldsSAQYSLSSDLPVTPTLdsLANSGIVFDNLW-ATPACSPTRATILTGKYGFRTGV--LAVPDELLL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 108 awQKTAEPFAFPVYLNKMRYQTFYCGKYlnQYGSKDAGGVAhvPPGWDQWHALVGN--SKYYNYTLSVNGKEEKHgDSYE 185
Cdd:cd16154 78 --SEETLLQLLIKDATTAGYSSAVIGKW--HLGGNDNSPNN--PGGIPYYAGILGGgvQDYYNWNLTNNGQTTNS-TEYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 186 KDYLTDLvlnrSLHFLEERspSHPFFMMLCPPAPHSPWTAAPQ--YSGSFSGVKAPRNgsfnkpgtdkhwllrqpANPMP 263
Cdd:cd16154 151 TTKLTNL----AIDWIDQQ--TKPWFLWLAYNAPHTPFHLPPAelHSRSLLGDSADIE-----------------ANPRP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 264 NssidYLdnafrrrwQTLLSVDDLVERLLKKLDSvKELDNTYIFYTSDHGyhT-GQ-----FSLPIDKRQLYEFDIRIPL 337
Cdd:cd16154 208 Y----YL--------AAIEAMDTEIGRLLASIDE-EERENTIIIFIGDNG--TpGQvvdlpYTRNHAKGSLYEGGINVPL 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1000814517 338 LVRGPGIKAKQTLQSPVLNI-DLPMTILDIAGVNLSTVNmDGQSFLP 383
Cdd:cd16154 273 IVSGAGVERANERESALVNAtDLYATIAELAGVDAAEIH-DSVSFKP 318
|
|
| PRK13759 |
PRK13759 |
arylsulfatase; Provisional |
30-409 |
1.57e-23 |
|
arylsulfatase; Provisional
Pssm-ID: 237491 [Multi-domain] Cd Length: 485 Bit Score: 103.60 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 30 SSKNNIILILTDDQ-DEQMGGM------TPmkkTRELIGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNH-LVHNNSVe 101
Cdd:PRK13759 4 TKKPNIILIMVDQMrGDCLGCNgnkaveTP---NLDMLASEGYNFENAYSAVPSCTPARAALLTGLSQWHHgRVGYGDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 102 gncssAAWQKTAEpfaFPVYLNKMRYQTFYCGKylnqygskdaggvAHVPPGWDQ--WHALVGNSKYynytLSVNGKEEK 179
Cdd:PRK13759 80 -----VPWNYKNT---LPQEFRDAGYYTQCIGK-------------MHVFPQRNLlgFHNVLLHDGY----LHSGRNEDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 180 HGDSYEKDYL--------------TDLVLN------------RSLH-----------FLEERSPSHPFFMMLCPPAPHSP 222
Cdd:PRK13759 135 SQFDFVSDYLawlrekapgkdpdlTDIGWDcnswvarpwdleERLHptnwvgsesieFLRRRDPTKPFFLKMSFARPHSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 223 WTAAPQYSGSFSGVKAPRNGSFNKPGTDKHWLLR-QPANPMPNSSIDYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKEL 301
Cdd:PRK13759 215 YDPPKRYFDMYKDADIPDPHIGDWEYAEDQDPEGgSIDALRGNLGEEYARRARAAYYGLITHIDHQIGRFLQALKEFGLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 302 DNTYIFYTSDHGYHTGQFSLpIDKRQLYEFDIRIPLLVRGPG----IKAKQTLQSPVLNIDLPMTILDIAGVNLSTVnMD 377
Cdd:PRK13759 295 DNTIILFVSDHGDMLGDHYL-FRKGYPYEGSAHIPFIIYDPGgllaGNRGTVIDQVVELRDIMPTLLDLAGGTIPDD-VD 372
|
410 420 430
....*....|....*....|....*....|..
gi 1000814517 378 GQSFLPqmAPSLRNGTERPFFLVEYTgEGYSS 409
Cdd:PRK13759 373 GRSLKN--LIFGQYEGWRPYLHGEHA-LGYSS 401
|
|
| GALNS_like |
cd16026 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
34-385 |
8.53e-22 |
|
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: 97.25 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMG-------GmTPMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYP-----HNHLVHNNS 99
Cdd:cd16026 3 NIVVILADD----LGygdlgcyG-SPLIKTPNIdrLAAEGVRFTDFYAAAPVCSPSRAALLTGRYPvrvglPGVVGPPGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 100 VEGncssaawQKTAEPFaFPVYLNKMRYQTFYCGKY----------LNQ-----YGskdaggvahVPPGWDQWHALVGNS 164
Cdd:cd16026 78 KGG-------LPPDEIT-IAEVLKKAGYRTALVGKWhlghqpeflpTRHgfdeyFG---------IPYSNDMWPFPLYRN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 165 KYYNYTLSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEeRSPSHPFFMMLCPPAPHSPWTAAPqysgSFSGVKapRNGsf 244
Cdd:cd16026 141 DPPGPLPPLMENEEVIEQPADQSSLTQRYTDEAVDFIE-RNKDQPFFLYLAHTMPHVPLFASE----KFKGRS--GAG-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 245 nkpgtdkhwllrqpanpmpnssiDYLDnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHG-----YHTGQF 319
Cdd:cd16026 212 -----------------------LYGD--------VVEELDWSVGRILDALKELGLEENTLVIFTSDNGpwleyGGHGGS 260
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 320 SLPID--KRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNL-STVNMDGQSFLPQM 385
Cdd:cd16026 261 AGPLRggKGTTWEGGVRVPFIAWWPGvIPAGTVSDELASTMDLLPTLAALAGAPLpEDRVIDGKDISPLL 330
|
|
| sulfatase_like |
cd16035 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
34-386 |
9.53e-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: 293759 [Multi-domain] Cd Length: 311 Bit Score: 95.74 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDdqdeQMGGMTPMK--------KTRELIGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNsvegncS 105
Cdd:cd16035 2 NILLILTD----QERYPPPWPagwaalnlPARERLAANGLSFENHYTAACMCSPSRSTLYTGLHPQQTGVTDT------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 106 SAAWQKTAEPfAFPVYLNKMR---YQTFYCGKylnqygskdaggvahvppgwdqWHalvgnskyynytLSvngkeEKHGD 182
Cdd:cd16035 72 GSPMQPLLSP-DVPTLGHMLRaagYYTAYKGK----------------------WH------------LS-----GAAGG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 183 SYEKDyltDLVLNRSLHFLEERSPSH----PFFMMLcppaphspwtaapqysgSFsgvkaprngsfnkpgtdkhwllrqp 258
Cdd:cd16035 112 GYKRD---PGIAAQAVEWLRERGAKNadgkPWFLVV-----------------SL------------------------- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 259 ANP---MpnssidyLDNAFRRRWQTLLS--------VDDLVERLLKKLDSVKELDNTYIFYTSDHG----YHTGqfslpi 323
Cdd:cd16035 147 VNPhdiM-------FPPDDEERWRRFRNfyynlirdVDRQIGRVLDALDASGLADNTIVVFTSDHGemggAHGL------ 213
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1000814517 324 dKRQ---LYEFDIRIPLLVRGPGIKAK-QTLQSPVLNIDLPMTILDIAGVNLSTVNMD-----GQSFLPQMA 386
Cdd:cd16035 214 -RGKgfnAYEEALHVPLIISHPDLFGTgQTTDALTSHIDLLPTLLGLAGVDAEARATEapplpGRDLSPLLT 284
|
|
| 4-S |
cd16029 |
N-acetylgalactosamine 4-sulfatase, also called arylsulftase B; Sulfatases catalyze the ... |
34-396 |
1.29e-21 |
|
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: 96.85 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDqdeqMG-----------GMTPmkKTRELIGDaGATFSNAFTStPLCCPSRSSFLSGRYPHnHLVHNNSVEG 102
Cdd:cd16029 2 HIVFILADD----LGwndvgfhgsdqIKTP--NLDALAAD-GVILNNYYVQ-PICTPSRAALMTGRYPI-HTGMQHGVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 103 NCSSAAWQKTaEPFaFPVYLNKMRYQTFYCGKY-LNQYGSKdaggvaHVPP--GWD---------QWHALVGNSKYYNYT 170
Cdd:cd16029 73 AGEPYGLPLN-ETL-LPQYLKELGYATHLVGKWhLGFYTWE------YTPTnrGFDsfygyyggaEDYYTHTSGGANDYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 171 LSVNGKEEKHGDSYEKDYLTDLVLNRSLHFLEERSPSHPFFMMLCPPAPHSPWTAAPQYsgsfsgvkaprngsfnkpgtd 250
Cdd:cd16029 145 NDDLRDNEEPAWDYNGTYSTDLFTDRAVDIIENHDPSKPLFLYLAFQAVHAPLQVPPEY--------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 251 khwllrQPANPMPNSSIDYLDnafRRRWQTLLS-VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSL----PI-- 323
Cdd:cd16029 204 ------ADPYEDKFAHIKDED---RRTYAAMVSaLDESVGNVVDALKAKGMLDNTLIVFTSDNGGPTGGGDGgsnyPLrg 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 324 DKRQLYEFDIRIPLLVRGPGIKAKqtlqSPVLN------ID-LPmTILDIAGVN-LSTVNMDGQSflpqMAPSLRNGTER 395
Cdd:cd16029 275 GKNTLWEGGVRVPAFVWSPLLPPK----RGTVSdglmhvTDwLP-TLLSLAGGDpDDLPPLDGVD----QWDALSGGAPS 345
|
.
gi 1000814517 396 P 396
Cdd:cd16029 346 P 346
|
|
| ARSK |
cd16171 |
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ... |
34-470 |
3.81e-19 |
|
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: 89.14 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDDQDEQMGGMtPMKKTREL-----IGDAGATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHNNSvegncssaa 108
Cdd:cd16171 2 NVVMVMSDSFDGRLTFR-PGNQVVDLpyinfMKQHGSVFLNAYTNSPICCPSRAAMWSGLFTHLTESWNNY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 109 wqKTAEPfAFPVYLNKMRYQtfycGKYLNQYGSKDAGGVAH-VPPGWDQWhalvgnSKYYNYTLSVNGK-------EEKH 180
Cdd:cd16171 72 --KGLDP-NYPTWMDRLEKH----GYHTQKYGKLDYTSGHHsVSNRVEAW------TRDVPFLLRQEGRptvnlvgDRST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 181 GDSYEKDY-LTDLvlnrSLHFLEERSPSH--PFFMMLCPPAPHsPWtAAPQYSGSFSGVKAPRngsfnkpgtdkhwllrq 257
Cdd:cd16171 139 VRVMLKDWqNTDK----AVHWIRKEAPNLtqPFALYLGLNLPH-PY-PSPSMGENFGSIRNIR----------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 258 panpmpnssidyldnAFRrrWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGyhtgqfSLPIDKRQ-----LYEFD 332
Cdd:cd16171 196 ---------------AFY--YAMCAETDAMLGEIISALKDTGLLDKTYVFFTSDHG------ELAMEHRQfykmsMYEGS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 333 IRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLsTVNMDGQSFLPQMAPSLRNGTER-----PFFLVEYTGegy 407
Cdd:cd16171 253 SHVPLLIMGPGIKAGQQVSDVVSLVDIYPTMLDIAGVPQ-PQNLSGYSLLPLLSESSIKESPSrvphpDWVLSEFHG--- 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000814517 408 ssqdpsCpklgpglaecfpdcvceDAFNNTYacvrTLKGANLQYCEFAD-NEAFVEMYNLTADP 470
Cdd:cd16171 329 ------C-----------------NVNASTY----MLRTNSWKYIAYADgNSVPPQLFDLSKDP 365
|
|
| ARS_like |
cd16142 |
uncharacterized arylsulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters ... |
34-379 |
6.55e-18 |
|
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: 85.28 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTDD----------QDEQMGGMTP-MKKtrelIGDAGATFSNaFTSTPLCCPSRSSFLSGRYPhnhlvhnnsVEG 102
Cdd:cd16142 2 NILVILGDDigwgdlgcygGGIGRGAPTPnIDR----LAKEGLRFTS-FYVEPSCTPGRAAFITGRHP---------IRT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 103 NCSSAAWQK-----TAEPFAFPVYLNKMRYQTFYCGKylNQYGSKDaggvAHVPP--GWDQWHAlvgnskYYNYTLsvng 175
Cdd:cd16142 68 GLTTVGLPGspgglPPWEPTLAELLKDAGYATAQFGK--WHLGDED----GRLPTdhGFDEFYG------NLYHTI---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 176 keekhgDsyekDYLTDlvlnRSLHFLEERSPS-HPFFMMLCPPAPHSPWTAAPQYSGsfsgvKAPRNGsfnkpgtdkhwl 254
Cdd:cd16142 132 ------D----EEIVD----KAIDFIKRNAKAdKPFFLYVNFTKMHFPTLPSPEFEG-----KSSGKG------------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 255 lrqpanpmpnssiDYLDnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHtgQFSLPI--------DKR 326
Cdd:cd16142 181 -------------KYAD--------SMVELDDHVGQILDALDELGIADNTIVIFTTDNGPE--QDVWPDggytpfrgEKG 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1000814517 327 QLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLSTVNMDGQ 379
Cdd:cd16142 238 TTWEGGVRVPAIVRWPGkIKPGRVSNEIVSHLDWFPTLAALAGAPDPKDKLLGK 291
|
|
| sulfatase_like |
cd16153 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
32-378 |
6.47e-16 |
|
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: 78.19 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDDQ--D--EQMGGMTPMKKTRELIG------DA----GATFSNAFTSTPLCCPSRSSFLSGRYPHNHLVHN 97
Cdd:cd16153 1 KPNILWIITDDQrvDslSCYNNAHTGKSESRLGYvespniDAlaaeGVLFTNAYCNSPVCVPSRTSMLTGRYPHRTGVYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 98 NsvegncsSAAWQKTAEPF-AFPVYLNKMRYQTFYCGK-YLNQYGSKdaggvahvppgwdqwhaLVGNSKYYNytlSVNG 175
Cdd:cd16153 81 F-------EAAHPALDHGLpTFPEVLKKAGYQTASFGKsHLEAFQRY-----------------LKNANQSYK---SFWG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 176 KEEKHGDSyekdyltdlvlnrslhfleerspSHPFFMMLCPPAPHSPwtaapqysgsfsgVKAPrngsfnkpgtdKHWLL 255
Cdd:cd16153 134 KIAKGADS-----------------------DKPFFVRLSFLQPHTP-------------VLPP-----------KEFRD 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 256 RqpanpmpnssIDYldNAFrrrwqtLLSVDDLVERLLKKLDSVKEL---DNTYIFYTSDHGYHTGQFSLpIDKRQLYEFD 332
Cdd:cd16153 167 R----------FDY--YAF------CAYGDAQVGRAVEAFKAYSLKqdrDYTIVYVTGDHGWHLGEQGI-LAKFTFWPQS 227
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1000814517 333 IRIPLLVRGPGIK---AKQTLQSPVLNIDLPMTILDIAGVNLSTVN-MDG 378
Cdd:cd16153 228 HRVPLIVVSSDKLkapAGKVRHDFVEFVDLAPTLLAAAGVDVDAPDyLDG 277
|
|
| spARS_like |
cd16160 |
sea urchin arylsulfatase-like; This family includes sea urchin arylsulfatase and its ... |
32-475 |
2.96e-15 |
|
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: 77.86 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDDQ---DEQMGGmtpmKKTRE--LIGD---AGATFSNAFTSTPLCCPSRSSFLSGRYPHnhlvHNNSVEGN 103
Cdd:cd16160 1 KPNIVLFFADDMgygDLASYG----HPTQErgPIDDmaaEGIRFTQAYSADSVCTPSRAALLTGRLPI----RSGMYGGT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 104 CSSAAWQKTAEP---FAFPVYLNKMRYQTFYCGKY---LNQYGSKDAggvAHVPP--GWD----------QW-------- 157
Cdd:cd16160 73 RVFLPWDIGGLPkteVTMAEALKEAGYTTGMVGKWhlgINENNHSDG---AHLPShhGFDfvgtnlpftnSWacddtgrh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 158 --HALVGNSKYYNYTLSVNgkeekhgDSYEKDYLTDLVLNRSLHFLEERSpSHPFFMMLCPPAPHSPWTAAPQYSGSfsg 235
Cdd:cd16160 150 vdFPDRSACFLYYNDTIVE-------QPIQHEHLTETLVGDAKSFIEDNQ-ENPFFLYFSFPQTHTPLFASKRFKGK--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 236 vkaPRNGSfnkpgtdkhwllrqpanpmpnssidYLDNAFRRRWQTLLSVDDLVErllKKLDsvkelDNTYIFYTSDHGYH 315
Cdd:cd16160 219 ---SKRGR-------------------------YGDNINEMSWAVGEVLDTLVD---TGLD-----QNTLVFFLSDHGPH 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 316 -----TGQFSLPID--KRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNIDLPMTILDIAGVNLST-VNMDGQSflpqMAP 387
Cdd:cd16160 263 veyclEGGSTGGLKggKGNSWEGGIRVPFIAYWPGTIKPRVSHEVVSTMDIFPTFVDLAGGTLPTdRIYDGLS----ITD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 388 SLRNGTERP----FFLVE----------YTGEGYSSQDPSCPKLGPglaECFPDCVCEDAFnntyacvrtlkganlqYCE 453
Cdd:cd16160 339 LLLGEADSPhddiLYYCCsrlmavrygsYKIHFKTQPLPSQESLDP---NCDGGGPLSDYI----------------VCY 399
|
490 500 510
....*....|....*....|....*....|
gi 1000814517 454 FADNEAFVE-----MYNLTADP---HQLEN 475
Cdd:cd16160 400 DCEDECVTKhnpplIFDVEKDPgeqYPLQP 429
|
|
| GALNS |
cd16157 |
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS); Lysosomal ... |
32-398 |
1.30e-14 |
|
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: 75.97 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDDqdeqMG----GM--TPMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHNNSVEG 102
Cdd:cd16157 1 KPNIILMLMDD----MGwgdlGVfgEPSRETPNLdrMAAEGMLFTDFYSANPLCSPSRAALLTGRLPiRNGFYTTNAHAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 103 NCSSAAWQKTAEP---FAFPVYLNKMRYQTFYCGKYlnqygskdagGVAHVPP------GWDQW-------HALVGNSKY 166
Cdd:cd16157 77 NAYTPQNIVGGIPdseILLPELLKKAGYRNKIVGKW----------HLGHRPQyhplkhGFDEWfgapnchFGPYDNKAY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 167 YNytLSVNGKEEKHGDSYE---------KDYLTDLVLNRSLHFLE-ERSPSHPFFMMLCPPAPHSPWTAAPQYSGSfsgv 236
Cdd:cd16157 147 PN--IPVYRDWEMIGRYYEefkidkktgESNLTQIYLQEALEFIEkQHDAQKPFFLYWAPDATHAPVYASKPFLGT---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 237 kaPRNGSFNkpgtdkhwllrqpanpmpnssidyldnafrrrwQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHT 316
Cdd:cd16157 221 --SQRGLYG---------------------------------DAVMELDSSVGKILESLKSLGIENNTFVFFSSDNGAAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 317 gqFSLPID----------KRQLYEFDIRIPLLVRGPGIKAKQTLQSPVLNI-DLPMTILDIAGVNLST-VNMDGQSFLpq 384
Cdd:cd16157 266 --ISAPEQggsngpflcgKQTTFEGGMREPAIAWWPGHIKPGQVSHQLGSLmDLFTTSLALAGLPIPSdRAIDGIDLL-- 341
|
410
....*....|....*.
gi 1000814517 385 maPSLRNGTE--RPFF 398
Cdd:cd16157 342 --PVLLNGKEkdRPIF 355
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
34-367 |
5.19e-12 |
|
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: 65.52 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 34 NIILILTD----DQDEQMGGMTPMKKTRELIGDAGATFsNAFTSTPLC--CPSRSSFLSGRYPHNHLV--HNNSVEGNCS 105
Cdd:cd00016 2 HVVLIVLDglgaDDLGKAGNPAPTTPNLKRLASEGATF-NFRSVSPPTssAPNHAALLTGAYPTLHGYtgNGSADPELPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 106 SAAWQKTAEPFaFPVYLNKMRYQTfycgkylnqygskdaggvahvppgwdqwhALVGNSKYynytlsvngkeekhgdsye 185
Cdd:cd00016 81 RAAGKDEDGPT-IPELLKQAGYRT-----------------------------GVIGLLKA------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 186 kdyltdlvlnrslhfLEERSPSHPFFMMLCPPAPHspwtaapqysgsfsgvkaprnGSFNKPGTDkhwllrqpanpmPNS 265
Cdd:cd00016 112 ---------------IDETSKEKPFVLFLHFDGPD---------------------GPGHAYGPN------------TPE 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 266 SIDyldnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHG---YHTGQFSLPIDKRQLYEFDIRIPLLVRGP 342
Cdd:cd00016 144 YYD-----------AVEEIDERIGKVLDALKKAGDADDTVIIVTADHGgidKGHGGDPKADGKADKSHTGMRVPFIAYGP 212
|
330 340
....*....|....*....|....*
gi 1000814517 343 GIKAKQTLQSPVLNIDLPMTILDIA 367
Cdd:cd00016 213 GVKKGGVKHELISQYDIAPTLADLL 237
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
268-382 |
8.66e-10 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 61.21 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 268 DYLDNAFRRRWQTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYefdiRIPLLVRGPGIKAK 347
Cdd:COG1368 410 DYGKTTLNNYLNAVRYADQALGEFIEKLKKSGWYDNTIFVIYGDHGPRSPGKTDYENPLERY----RVPLLIYSPGLKKP 485
|
90 100 110
....*....|....*....|....*....|....*
gi 1000814517 348 QTLQSPVLNIDLPMTILDIAGVNLSTVNMDGQSFL 382
Cdd:COG1368 486 KVIDTVGSQIDIAPTLLDLLGIDYPSYYAFGRDLL 520
|
|
| ES |
cd16159 |
Estrone sulfatase; Human estrone sulfatase (ES) is responsible for maintaining high levels of ... |
288-404 |
3.64e-07 |
|
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: 52.68 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 288 VERLLKKLDSVKELDNTYIFYTSDHGYHTGQfslpIDKRQLYE--------------FD--IRIPLLVRGPG-IKAKQTL 350
Cdd:cd16159 292 VGQILDALDELGLKDNTFVYFTSDNGGHLEE----ISVGGEYGggnggiyggkkmggWEggIRVPTIVRWPGvIPPGSVI 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1000814517 351 QSPVLNIDLPMTILDIAGVNLST-VNMDGQSFLPQmapsLRNGTERPF--FLVEYTG 404
Cdd:cd16159 368 DEPTSLMDIFPTVAALAGAPLPSdRIIDGRDLMPL----LTGQEKRSPheFLFHYCG 420
|
|
| ARSG |
cd16161 |
arylsulfatase G; Arylsulfatase G is a subfamily of sulfatases which specifically hydrolyze ... |
32-373 |
6.70e-07 |
|
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: 51.32 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 32 KNNIILILTDD---QDEQMGGMTPMKKTREL--IGDAGATFSNAFTSTPLCCPSRSSFLSGRYP-HNHLVHN---NSVEG 102
Cdd:cd16161 1 KPNFLLLFADDlgwGDLGANWAPNAILTPNLdkLAAEGTRFVDWYSAASVCSPSRASLMTGRLGlRNGVGHNflpTSVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 103 ---NCSSAAWQktaepfafpvyLNKMRYQTFYCGKY-LNQYGskdaggvAHVPpgwdqwhalvgNSKYYNYTLSVNGKEE 178
Cdd:cd16161 81 lplNETTLAEV-----------LRQAGYATGMIGKWhLGQRE-------AYLP-----------NSRGFDYYFGIPFSHD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 179 KH-GDSYeKDYLTDLVLNRSlhfleerSPSHPFFMMLCPPAPHSPWTAAPQysgsfsgvkaprngsfnkpgtdkhwllrq 257
Cdd:cd16161 132 SSlADRY-AQFATDFIQRAS-------AKDRPFFLYAALAHVHVPLANLPR----------------------------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 258 PANPMPNSSIdYLDnafrrrwqTLLSVDDLVERLLKKLDSVKELDNTYIFYTSD---------------HGYHTGQFSLP 322
Cdd:cd16161 175 FQSPTSGRGP-YGD--------ALQEMDDLVGQIMDAVKHAGLKDNTLTWFTSDngpwevkcelavgpgTGDWQGNLGGS 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1000814517 323 IDKRQLYEFDIRIPLLVRGPG-IKAKQTLQSPVLNIDLPMTILDIAGVNLST 373
Cdd:cd16161 246 VAKASTWEGGHREPAIVYWPGrIPANSTSAALVSTLDIFPTVVALAGASLPP 297
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
285-368 |
1.18e-06 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 49.99 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 285 DDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFSLPIDKRQLYEFdiRIPLLVRGPGIKAKQTLQSPVLNIDLPMTIL 364
Cdd:cd16015 202 DKALGEFIEKLKKSGLYENTIIVIYGDHLPSLGSDYDETDEDPLDLY--RTPLLIYSPGLKKPKKIDRVGSQIDIAPTLL 279
|
....
gi 1000814517 365 DIAG 368
Cdd:cd16015 280 DLLG 283
|
|
| YejM |
COG3083 |
Periplasmic protein PbgA/YejM, regulator of the LPS biosynthesis, AlkP superfamily [Cell wall ... |
200-364 |
2.48e-06 |
|
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: 49.90 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 200 FLEERSPSHPFFmmlcppaphspwtaapqysgSFSGVKAPRNGSFNKPgtdkHWLLRQPANPMPNSSIDYLDNA--FRRR 277
Cdd:COG3083 373 WLDQRDSDRPWF--------------------SYLFLDAPHAYSFPAD----YPKPFQPSEDCNYLALDNESDPtpFKNR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 278 WQT-LLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGY-----------HTGQFSlpidkrqlyEFDIRIPLLVRGPGiK 345
Cdd:COG3083 429 YRNaVHYVDSQIGRVLDTLEQRGLLENTIVIITADHGEefnengqnywgHNSNFS---------RYQLQVPLVIHWPG-T 498
|
170
....*....|....*....
gi 1000814517 346 AKQTLQSPVLNIDLPMTIL 364
Cdd:COG3083 499 PPQVISKLTSHLDIVPTLM 517
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
279-368 |
6.20e-05 |
|
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: 44.88 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 279 QTLLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHT----GQFSlpidkrqlYEFDIRIPLLVRGPGIKAKQTLQsPV 354
Cdd:cd16018 183 EALKRVDRRLGYLIEALKERGLLDDTNIIVVSDHGMTDvgthGYDN--------ELPDMRAIFIARGPAFKKGKKLG-PF 253
|
90
....*....|....
gi 1000814517 355 LNIDLPMTILDIAG 368
Cdd:cd16018 254 RNVDIYPLMCNLLG 267
|
|
| LptA |
cd16017 |
Lipooligosaccharide Phosphoethanolamine Transferase A (LptA) or Lipid A Phosphoethanolamine ... |
280-370 |
7.53e-05 |
|
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: 44.54 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 280 TLLSVDDLVERLLKKLDSVKEldNTYIFYTSDHG---YHTGQF--SLPIDKRQLYEfdirIPLLV--------RGPGIKA 346
Cdd:cd16017 191 SILYTDYVLSQIIERLKKKDK--DAALIYFSDHGeslGENGLYlhGAPYAPKEQYH----VPFIIwssdsykqRYPVERL 264
|
90 100
....*....|....*....|....
gi 1000814517 347 KQTLQSPVLNIDLPMTILDIAGVN 370
Cdd:cd16017 265 RANKDRPFSHDNLFHTLLGLLGIK 288
|
|
| ALP_like |
cd16021 |
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific ... |
266-367 |
1.68e-04 |
|
uncharacterized Alkaline phosphatase subfamily; Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity.
Pssm-ID: 293745 Cd Length: 278 Bit Score: 43.28 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 266 SIDYLDNAFRrrwqtllsVDDLVERLLKKLDSVKELDNTYIFYTSDHGY--------HTGQF--SLPIdkrqLYefdIRI 335
Cdd:cd16021 175 THDYLNGLSL--------ADEDLLEFLKRLKENGLLDNTFVIFMSDHGLrfgkiretLQGKLeeRLPF----LS---ISL 239
|
90 100 110
....*....|....*....|....*....|....*....
gi 1000814517 336 P--LLVRGPGIKA-----KQTLQSPvlnIDLPMTILDIA 367
Cdd:cd16021 240 PkwFREKYPEAVAnlkknSNRLTTP---FDLHATLLDIL 275
|
|
| ARSA |
cd16158 |
Arylsulfatase A or cerebroside-sulfatase; Arylsulfatase A breaks down sulfatides, namely ... |
281-391 |
2.27e-04 |
|
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: 43.59 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 281 LLSVDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFS-------LPIDKRQLYEFDIRIPLLVRGPG-IKAKQT--L 350
Cdd:cd16158 232 LAELDGSVGELLQTLKENGIDNNTLVFFTSDNGPSTMRKSrggnaglLKCGKGTTYEGGVREPAIAYWPGrIKPGVTheL 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1000814517 351 QSpvlNIDLPMTILDIAGVNLSTVNMDGQSFLP---QMAPSLRN 391
Cdd:cd16158 312 AS---TLDILPTIAKLAGAPLPNVTLDGVDMSPilfEQGKSPRQ 352
|
|
| DUF229 |
pfam02995 |
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are ... |
274-391 |
3.48e-03 |
|
Protein of unknown function (DUF229); Members of this family are uncharacterized. They are 500-1200 amino acids in length and share a long region conservation that probably corresponds to several domains. The Go annotation for the protein indicates that it is involved in nematode larval development and has a positive regulation on growth rate.
Pssm-ID: 397236 Cd Length: 496 Bit Score: 40.02 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814517 274 FRRRWQTLLS---------VDDLVERLLKKLDSVKELDNTYIFYTSDHGYHTGQFslpidkRQLYE--FDIRIPLLVRG- 341
Cdd:pfam02995 294 FGFFWSNSLShddfnyasaLDEDFLKYLKKLHKRGLLDNTIVIFMSDHGLRFGKL------RRTSQgmLEERLPLMSIRy 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1000814517 342 -PGIKAK-----QTLQSP----VLNIDLPMTILDIAGVNLSTVNMD-----------GQS-FLPQmaPSLRN 391
Cdd:pfam02995 368 pPWFRETypqavENLELNanrlTTPFDLHATLKDILHLGELSDKELqdrmkaldcprGISlFLPI--PDNRT 437
|
|
| |
